Sandbox Reserved 779: Difference between revisions
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===Lipocalin Proteins=== | ===Lipocalin Proteins=== | ||
Lipocalins are typically small (160-180 residues in length), extracellular proteins sharing several common molecular recognition properties: the binding of small, principally hydrophobic molecules (such as retinol); binding to speci¢c cell-surface receptors; and the formation of covalent and non-covalent complexes with other soluble macromolecules. Although they have been classified mainly as transport proteins | |||
<ref>PMID:11058743</ref> | |||
== Structure of β-LG == | == Structure of β-LG == | ||
At physiological conditions, bovine b-lactoglobulin forms a dimer, with each monomer consisting of 162 amino acid residues and characterized by a molecular mass of 18,350.1 Below pH 3, the dimer dissociates into monomers which preserve their native conformation.2±4 Genetically, b-lactoglobulin may exist as one of several variants, among which the variants A and B are the most abundant.1 The A and B variants of the protein differ from each other by amino acid residues at positions Asp64 (Gly64 in variant B) and Val118 (Ala118 in variant B). These differences in primary structure render the two variants slightly different with respect to isoelectric point, solubility, self-association properties, as well as pressure and temperature stability.5±7 However, the structural characteristics of the A and B variants of bovine b-lactoglobulin are virtually indistinguishable.8 In its native state, b-lactoglobulin is a predominantly b-sheet protein containing nine b-strands and three a-helices.8±10 The core of the protein is formed by a ¯attened b-barrel (a calyx) composed of eight antiparallel b-strands (A to H). <ref>PMID:11734004</ref> | |||
βLG consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol | βLG consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol | ||
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solvent in the native structure, making them useful probes for monitoring site-specific conformational changes. In addition, studies | solvent in the native structure, making them useful probes for monitoring site-specific conformational changes. In addition, studies | ||
on the monomer–dimer equilibrium [30,32,42,43] and the reactivity of the thiol group of Cys121 deeply buried between the α-helix and H | on the monomer–dimer equilibrium [30,32,42,43] and the reactivity of the thiol group of Cys121 deeply buried between the α-helix and H | ||
strand [44–48] revealed other important properties of βLG. | strand [44–48] revealed other important properties of βLG.<ref>PMID:19362581</ref> | ||
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protein fold and how thats important for the function | protein fold and how thats important for the function | ||
ligands if theres ligands | ligands if theres ligands | ||
the active site if relevant | the active site if relevant | ||
features of protein that are important for function | features of protein that are important for function | ||
zoom in on the active site, label the important active site residues, and hughlight those residues in a different color (make it look pretty) | zoom in on the active site, label the important active site residues, and hughlight those residues in a different color (make it look pretty) | ||
==Mechanism of action== | ==Mechanism of action== | ||
===how the protein function=== | ===how the protein function=== | ||
include chemical structure of any relevant ligands, inhibitors, or important states in the reaction pathway. | include chemical structure of any relevant ligands, inhibitors, or important states in the reaction pathway. | ||
==Implications or possible application== | ==Implications or possible application== | ||
describe any uses or application that have been made of the protein | describe any uses or application that have been made of the protein | ||
