1b0o: Difference between revisions
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==BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z== | ==BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z== | ||
<StructureSection load='1b0o' size='340' side='right' caption='[[1b0o]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1b0o' size='340' side='right'caption='[[1b0o]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b0o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B0O FirstGlance]. <br> | <table><tr><td colspan='2'>[[1b0o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B0O FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/1b0o_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/1b0o_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1b0o" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1b0o" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Sawyer, L]] | [[Category: Sawyer, L]] | ||
[[Category: Wu, S Y]] | [[Category: Wu, S Y]] | ||
Revision as of 20:53, 14 August 2019
BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE ZBOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z
Structural highlights
Function[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBovine beta-lactoglobulin (beta-Lg) has been studied extensively in both the isolated and the naturally occurring states. It is a commercially important whey protein of obvious nutritional value but, so far, one that has no clearly identified biological function. In common with many of the other members of the lipocalin family to which it belongs, beta-Lg binds hydrophobic ligands, and it appears possible that there are at least two distinct binding sites per monomer for a variety of ligands. By comparison with other members of the family, there is a probable binding site in the central cavity of the molecule that is formed by the eight antiparallel beta-strands that are typical of the lipocalins. We have now cocrystallized beta-Lg with palmitic acid, and the refined structure (R = 0.204, Rfree = 0.240 for 6,888 reflections to 2.5-A resolution) reveals that the ligand binds in the central cavity in a manner similar to the binding of retinol to the related lipocalin, serum retinol-binding protein. The carboxyl group binds to both Lys-60 and Lys-69 at the entrance to the cavity. The hydrophobic tail stretches in an almost fully extended conformation into the center of the protein. This is the first direct observation of a ligand binding to beta-Lg. beta-lactoglobulin binds palmitate within its central cavity.,Wu SY, Perez MD, Puyol P, Sawyer L J Biol Chem. 1999 Jan 1;274(1):170-4. PMID:9867826[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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