1b0o
From Proteopedia
(New page: 200px<br /><applet load="1b0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0o, resolution 2.50Å" /> '''BOVINE BETA-LACTOGLO...) |
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| - | [[Image:1b0o.gif|left|200px]]<br /><applet load="1b0o" size=" | + | [[Image:1b0o.gif|left|200px]]<br /><applet load="1b0o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b0o, resolution 2.50Å" /> | caption="1b0o, resolution 2.50Å" /> | ||
'''BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z'''<br /> | '''BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bovine beta-lactoglobulin (beta-Lg) has been studied extensively in both | + | Bovine 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1B0O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with PLM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1B0O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sawyer, L.]] | [[Category: Sawyer, L.]] | ||
| - | [[Category: Wu, S | + | [[Category: Wu, S Y.]] |
[[Category: PLM]] | [[Category: PLM]] | ||
[[Category: bovine]] | [[Category: bovine]] | ||
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[[Category: palmitate-binding]] | [[Category: palmitate-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:17 2008'' |
Revision as of 09:50, 21 February 2008
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BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z
Overview
Bovine 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.
About this Structure
1B0O is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 11:50:17 2008
Categories: Bos taurus | Single protein | Sawyer, L. | Wu, S Y. | PLM | Bovine | Lipocalin | Milk whey protein | Palmitate-binding
