4gny

Bovine beta-lactoglobulin complex with dodecyl sulfate

spinqualitylabelsall models 4gny, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gny is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6367Å Ligands: GOL, SDS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMed Unlike most small globular proteins, lipocalins lack a compact hydrophobic core. Instead, they present a large central cavity that functions as the primary binding site for hydrophobic molecules. Not surprisingly, these proteins typically exhibit complex structural dynamics in solution, which is intricately modified by intermolecular recognition events. Although many lipocalins are monomeric, an increasing number of them have been proven to form oligomers. The coupling effects between self-association and ligand binding in these proteins are largely unknown. To address this issue, we have calorimetrically characterized the recognition of dodecyl sulfate by bovine beta-lactoglobulin, which forms weak homodimers at neutral pH. A thermodynamic analysis based on coupled-equilibria revealed that dimerization exerts disparate effects on the ligand-binding capacity of beta-lactoglobulin. Protein dimerization decreases ligand affinity (or, reciprocally, ligand binding promotes dimer dissociation). The two subunits in the dimer exhibit a positive, entropically driven cooperativity. To investigate the structural determinants of the interaction, the crystal structure of beta-lactoglobulin bound to dodecyl sulfate was solved at 1.64 A resolution. Copyright (c) 2013 John Wiley & Sons, Ltd. Ligand binding and self-association cooperativity of beta-lactoglobulin.,Gutierrez-Magdaleno G, Bello M, Portillo-Tellez MC, Rodriguez-Romero A, Garcia-Hernandez E J Mol Recognit. 2013 Feb;26(2):67-75. doi: 10.1002/jmr.2249. PMID:23334914 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactoglobulin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA