1gni
From Proteopedia
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|PDB= 1gni |SIZE=350|CAPTION= <scene name='initialview01'>1gni</scene>, resolution 2.40Å | |PDB= 1gni |SIZE=350|CAPTION= <scene name='initialview01'>1gni</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=OL1:Ola+Binding+Site+For+A1007'>OL1</scene> | |SITE= <scene name='pdbsite=OL1:Ola+Binding+Site+For+A1007'>OL1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=OLA:OLEIC ACID'>OLA</scene> | + | |LIGAND= <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gni OCA], [http://www.ebi.ac.uk/pdbsum/1gni PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gni RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts. | The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Analbuminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperzincemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Gruene, T.]] | [[Category: Gruene, T.]] | ||
[[Category: Petitpas, I.]] | [[Category: Petitpas, I.]] | ||
| - | [[Category: OLA]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
[[Category: lipid-binding]] | [[Category: lipid-binding]] | ||
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[[Category: plasma protein]] | [[Category: plasma protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:33 2008'' |
Revision as of 17:47, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-9-OCTADECENOIC ACID (OLEIC ACID)
Overview
The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts.
About this Structure
1GNI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids., Petitpas I, Grune T, Bhattacharya AA, Curry S, J Mol Biol. 2001 Dec 14;314(5):955-60. PMID:11743713
Page seeded by OCA on Sun Mar 30 20:47:33 2008
