1o1u: Difference between revisions

Revision as of 23:28, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1o1u.png

Template:STRUCTURE 1o1u

human ileal lipid-binding protein (ILBP) in free formhuman ileal lipid-binding protein (ILBP) in free form

Template:ABSTRACT PUBMED 12486725

About this StructureAbout this Structure

1O1U is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures., Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W, Proteins. 2003 Feb 1;50(2):312-28. PMID:12486725

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-'''human ileal lipid-binding protein (ILBP) in free form'''
+===human ileal lipid-binding protein (ILBP) in free form===
-==Overview==
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-Bile acids are generated in vivo from cholesterol in the liver, and they undergo an enterohepatic circulation involving the small intestine, liver, and kidney. To understand the molecular mechanism of this transportation, it is essential to gain insight into the three-dimensional (3D) structures of proteins involved in the bile acid recycling in free and complexed form and to compare them with homologous members of this protein family. Here we report the solution structure of the human ileal lipid-binding protein (ILBP) in free form and in complex with cholyltaurine. Both structures are compared with a previously published structure of the porcine ILBP-cholylglycine complex and with related lipid-binding proteins. Protein structures were determined in solution by using two-dimensional (2D)- and 3D-homo and heteronuclear NMR techniques, leading to an almost complete resonance assignment and a significant number of distance constraints for distance geometry and restrained molecular dynamics simulations. The identification of several intermolecular distance constraints unambiguously determines the cholyltaurine-binding site. The bile acid is deeply buried within ILBP with its flexible side-chain situated close to the fatty acid portal as entry region into the inner ILBP core. This binding mode differs significantly from the orientation of cholylglycine in porcine ILBP. A detailed analysis using the GRID/CPCA strategy reveals differences in favorable interactions between protein-binding sites and potential ligands. This characterization will allow for the rational design of potential inhibitors for this relevant system.
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+{{ABSTRACT_PUBMED_12486725}}
 ==About this Structure==
-O1U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O1U OCA].
+O1U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O1U OCA].
 ==Reference==
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 [[Category: Thuering, H.]]
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