Structures of nucleotide-bound and free aIF2γ from Sulfolobus
... required (Fig. 2a), whereas switch 2 predominantly retains its position. To bind GTP both the Ploop and switch 2 must change their conformations (Fig. 2b). It seems difficult to predict whether the conformational changes of the P-loop and switch 2 occur spontaneous, or promoted by nucleotide binding ...
... required (Fig. 2a), whereas switch 2 predominantly retains its position. To bind GTP both the Ploop and switch 2 must change their conformations (Fig. 2b). It seems difficult to predict whether the conformational changes of the P-loop and switch 2 occur spontaneous, or promoted by nucleotide binding ...
Novel eukaryotic enzymes modifying cell
... microbial eukaryotes, and cell walls and waxes of plants and fungi. Not only do these play a major structural role in both unicellular and multicellular eukaryotes, but they are also important in the defense against parasites or interactions of parasites with their hosts. The enzymatic components of ...
... microbial eukaryotes, and cell walls and waxes of plants and fungi. Not only do these play a major structural role in both unicellular and multicellular eukaryotes, but they are also important in the defense against parasites or interactions of parasites with their hosts. The enzymatic components of ...
Nerve activates contraction
... • Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. • This provides the structural strength for their role in ...
... • Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. • This provides the structural strength for their role in ...
Intrinsically unstructured proteins
... proper spatial organization of active site residues requires a rigid fold they cannot provide. Furthermore, their functions are invariably linked to their structural disorder and can be classified into 28 distinct categories. Here, it is suggested that they actually fall into five broad functional c ...
... proper spatial organization of active site residues requires a rigid fold they cannot provide. Furthermore, their functions are invariably linked to their structural disorder and can be classified into 28 distinct categories. Here, it is suggested that they actually fall into five broad functional c ...
Beta Structures
... Retinol is bound inside the barrel, between the two b sheets, such that its only hydrophilic part (an OH tail) is at the surface of the molecule. Exhibits only minimal conformational changes in both apo- (open) and holo- (bound) forms. ...
... Retinol is bound inside the barrel, between the two b sheets, such that its only hydrophilic part (an OH tail) is at the surface of the molecule. Exhibits only minimal conformational changes in both apo- (open) and holo- (bound) forms. ...
The Endoplasmic Reticulum Glucosyltransferase
... strates are glycoproteins, the original E7 in CI2 was replaced by a cysteine (E7C) to which a high mannose-type glycopeptide derived from bovine thyroglobulin was attached through a bifunctional chemical cross-linker (glycosylated CI2s are to be referred to as GCI2s). The original glutamic acid resi ...
... strates are glycoproteins, the original E7 in CI2 was replaced by a cysteine (E7C) to which a high mannose-type glycopeptide derived from bovine thyroglobulin was attached through a bifunctional chemical cross-linker (glycosylated CI2s are to be referred to as GCI2s). The original glutamic acid resi ...
Phenylketonuria (PKU)
... Catalytic Domain of Human Phenylalanine Hydroxylase in its Catalytically Active Fe(II) Form and Binary Complex with Tetrahydrobiopterin. J.Mol.Biol. 314; 266 H.Erlandsen, E.Bjorgo, T.Flatmark, R.C.Stevens(2000). Crystal Structure and SiteSpecific Mutagenesis of Pterin-Bound Human Phenylalanine Hydro ...
... Catalytic Domain of Human Phenylalanine Hydroxylase in its Catalytically Active Fe(II) Form and Binary Complex with Tetrahydrobiopterin. J.Mol.Biol. 314; 266 H.Erlandsen, E.Bjorgo, T.Flatmark, R.C.Stevens(2000). Crystal Structure and SiteSpecific Mutagenesis of Pterin-Bound Human Phenylalanine Hydro ...
Structural Characterization of Humanized Nanobodies with
... role during the early phase of infection [3,4]. CyaA is a 1706-residue long bi-functional protein which consists of an N-terminal adenylate cyclase (AC) catalytic domain (residues 1–400) and a C-terminal pore-forming or hemolysin (Hly) domain (residues 401–1706) [4]. Upon entry into the host cells, ...
... role during the early phase of infection [3,4]. CyaA is a 1706-residue long bi-functional protein which consists of an N-terminal adenylate cyclase (AC) catalytic domain (residues 1–400) and a C-terminal pore-forming or hemolysin (Hly) domain (residues 401–1706) [4]. Upon entry into the host cells, ...
The lower Vmax is consistent with the mutation resulting in a
... of tissue-specific receptor complexes involved in regulating cell adhesion, growth, and differentiation. These complexes contain a member of the tetraspanin superfamily of transmembrane proteins that is non-covalently associated with one or more membrane receptors or glycoproteins. The tetraspanins ...
... of tissue-specific receptor complexes involved in regulating cell adhesion, growth, and differentiation. These complexes contain a member of the tetraspanin superfamily of transmembrane proteins that is non-covalently associated with one or more membrane receptors or glycoproteins. The tetraspanins ...
Problem set answers
... 4. AlphaCP1 is a polyC/U binding protein that binds to polyC/U-containing 3' UTR regions of certain mRNA species to stabilize the message and suppress translation. Phosphorylation of aCP1 by S6 protein kinase is thought to result in reduced binding to the mRNA and release of the protein from the po ...
... 4. AlphaCP1 is a polyC/U binding protein that binds to polyC/U-containing 3' UTR regions of certain mRNA species to stabilize the message and suppress translation. Phosphorylation of aCP1 by S6 protein kinase is thought to result in reduced binding to the mRNA and release of the protein from the po ...
Intrinsic Protein Disorder and Protein
... Interestingly, our dataset indicates that protein disorder is involved in coregulatory proteins of nuclear receptors (NR) such as coactivators and corepressors, making it possible for them to perform one-to-many signaling and to function as disordered hubs. The nuclear receptors (NRs) are a super-fa ...
... Interestingly, our dataset indicates that protein disorder is involved in coregulatory proteins of nuclear receptors (NR) such as coactivators and corepressors, making it possible for them to perform one-to-many signaling and to function as disordered hubs. The nuclear receptors (NRs) are a super-fa ...
Slide 1
... FIGURE 9-8: Bidirectional integrin signaling. Integrins can signal in two directions. During inside-out signaling, intracellular activators, such as talin or kindlins, bind to the β-integrin tail, leading to conformational changes that result in integrin activation. Integrins can also behave like t ...
... FIGURE 9-8: Bidirectional integrin signaling. Integrins can signal in two directions. During inside-out signaling, intracellular activators, such as talin or kindlins, bind to the β-integrin tail, leading to conformational changes that result in integrin activation. Integrins can also behave like t ...
Full PDF
... (VL) combines with a variable domain of the heavy chain (V Hl in the antibody molecule to form the heterodimeric Fv fragment , the smallest immunoglobulin substructure that is fully competent to bind the antigen . A number of structures of immunoglobulin variable domains have been determined since t ...
... (VL) combines with a variable domain of the heavy chain (V Hl in the antibody molecule to form the heterodimeric Fv fragment , the smallest immunoglobulin substructure that is fully competent to bind the antigen . A number of structures of immunoglobulin variable domains have been determined since t ...
Protein folding: looping from hydrophobic nuclei.
... for the mapping of the loops. As it follows from comparisons with hydrophobicity plots not all hydrophobic sites participate in the linear arrangement of the nearly standard loops and their ends. The additional hydrophobic sites correspond, apparently, to secondary loop-to-loop interactions, that is ...
... for the mapping of the loops. As it follows from comparisons with hydrophobicity plots not all hydrophobic sites participate in the linear arrangement of the nearly standard loops and their ends. The additional hydrophobic sites correspond, apparently, to secondary loop-to-loop interactions, that is ...
Hydrocarbons: Mechanisms of Cellular Toxicity
... – Exerting similar or antagonistic effects – Something derived from same source or ...
... – Exerting similar or antagonistic effects – Something derived from same source or ...
Signal Transduction
... G-proteins are heterotrimeric, with 3 subunits a, b, g. A G-protein that activates cyclic-AMP formation within a cell is called a stimulatory G-protein, designated Gs with alpha subunit Gsa. Gs is activated, e.g., by receptors for the hormones epinephrine and glucagon. The b-adrenergic recept ...
... G-proteins are heterotrimeric, with 3 subunits a, b, g. A G-protein that activates cyclic-AMP formation within a cell is called a stimulatory G-protein, designated Gs with alpha subunit Gsa. Gs is activated, e.g., by receptors for the hormones epinephrine and glucagon. The b-adrenergic recept ...
A critical pocket close to the glutamate binding site of
... In 1993 P. O’Hara and colleagues were the first to demonstrate that both metabotropic glutamate receptors (mGluRs) and ionotropic glutamate receptors hold an amino terminal domain (ATD) that adopts the fold of LIVBP a bacterial periplasmic binding protein and that was thus named the LIVBP domain (O' ...
... In 1993 P. O’Hara and colleagues were the first to demonstrate that both metabotropic glutamate receptors (mGluRs) and ionotropic glutamate receptors hold an amino terminal domain (ATD) that adopts the fold of LIVBP a bacterial periplasmic binding protein and that was thus named the LIVBP domain (O' ...
Document
... turn allows binding of the virus to a specific subset of chemokine receptors on cell surface. Once bound to the chemokine receptor the trimeric gp120 protein springs open, projecting three peptide fusion domains that “harpoon” the lipid bilayer of the target cell. The fusion domains then form hair ...
... turn allows binding of the virus to a specific subset of chemokine receptors on cell surface. Once bound to the chemokine receptor the trimeric gp120 protein springs open, projecting three peptide fusion domains that “harpoon” the lipid bilayer of the target cell. The fusion domains then form hair ...
Day 2 Summary
... • A saturated fat will allow the fat molecules to align closer together, making these fats solid (at room temp) • An unsaturated fatty acid will have a kink in the tail; which prevents close packing of these fats, and so they tend to be liquid (at room temp) • Unsaturated fats can be mono- (one doub ...
... • A saturated fat will allow the fat molecules to align closer together, making these fats solid (at room temp) • An unsaturated fatty acid will have a kink in the tail; which prevents close packing of these fats, and so they tend to be liquid (at room temp) • Unsaturated fats can be mono- (one doub ...
Arfs and membrane lipids: sensing, generating and responding to
... with GTP and interact with effector proteins in a soluble form. However, interactions of truncated Arfs may not reflect the full extent and behaviour of Arfs in cells, which takes place on membrane surfaces. In this issue of the Biochemical Journal, Lundmark et al. [6] re-examine the interactions of ...
... with GTP and interact with effector proteins in a soluble form. However, interactions of truncated Arfs may not reflect the full extent and behaviour of Arfs in cells, which takes place on membrane surfaces. In this issue of the Biochemical Journal, Lundmark et al. [6] re-examine the interactions of ...
Signaling9
... G Protein Signal Cascade Most signal molecules targeted to a cell bind at the cell surface to receptors embedded in the plasma membrane. Only signal molecules able to cross the plasma membrane (e.g., steroid hormones) interact with intracellular receptors. A large family of cell surface receptors h ...
... G Protein Signal Cascade Most signal molecules targeted to a cell bind at the cell surface to receptors embedded in the plasma membrane. Only signal molecules able to cross the plasma membrane (e.g., steroid hormones) interact with intracellular receptors. A large family of cell surface receptors h ...
Lecture 6 Protein Tertiary and Quaternary Structure
... describe a protein in terms like "homotetramer", "heterodimer", etc. • Explain simple rotational symmetry for an oligomeric protein such as a homodimer like the Cro protein or a heterotetramer like hemoglobin. – Be able to use (correctly) the terms "2-fold", "3-fold", etc. to refer to simple rotatio ...
... describe a protein in terms like "homotetramer", "heterodimer", etc. • Explain simple rotational symmetry for an oligomeric protein such as a homodimer like the Cro protein or a heterotetramer like hemoglobin. – Be able to use (correctly) the terms "2-fold", "3-fold", etc. to refer to simple rotatio ...
antimicrobial drugs
... Be able to list enzymes produced by microbes than enhance pathogenicity and virulence as well as describe the effects of these enzymes on the host (i.e., hyaluronidase, collangenase, coagulase, kinase). ...
... Be able to list enzymes produced by microbes than enhance pathogenicity and virulence as well as describe the effects of these enzymes on the host (i.e., hyaluronidase, collangenase, coagulase, kinase). ...
Plant Molecular Biology
... a polypeptide of 251 amino acids which is much smaller than other DRPs. It is not known if DRP6 gene is transcribed, and if its encoded protein is a GTPase. We hope that these changes will make it easier to follow the exciting research on DRPs in plants. Unlike actins and tubulins that polymerize in ...
... a polypeptide of 251 amino acids which is much smaller than other DRPs. It is not known if DRP6 gene is transcribed, and if its encoded protein is a GTPase. We hope that these changes will make it easier to follow the exciting research on DRPs in plants. Unlike actins and tubulins that polymerize in ...
Anthrax toxin
Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis—the causative agent of anthrax. The toxin was first discovered by Harry Smith in 1954. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). These three protein components act together to impart their physiological effects. Assembled complexes containing the toxin components are endocytosed. In the endosome, the enzymatic components of the toxin translocate into the cytoplasm of a target cell. Once in the cytosol, the enzymatic components of the toxin disrupts various immune cell functions, namely cellular signaling and cell migration. The toxin may even induce cell lysis, as is observed for macrophage cells. Anthrax toxin allows the bacteria to evade the immune system, proliferate, and ultimately kill the host animal. Research on anthrax toxin also provides insight into the generation of macromolecular assemblies, and on protein translocation, pore formation, endocytosis, and other biochemical processes.