1bj5: Difference between revisions

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==Overview==
==Overview==
Human serum albumin (HSA) is the most abundant protein in the circulatory, system. Its principal function is to transport fatty acids, but it is also, capable of binding a great variety of metabolites and drugs. Despite, intensive efforts, the detailed structural basis of fatty acid binding to, HSA has remained elusive. We have now determined the crystal structure of, HSA complexed with five molecules of myristate at 2.5 A resolution. The, fatty acid molecules bind in long, hydrophobic pockets capped by polar, side chains, many of which are basic. These pockets are distributed, asymmetrically throughout the HSA molecule, despite its symmetrical, repeating domain structure.
Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has remained elusive. We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar side chains, many of which are basic. These pockets are distributed asymmetrically throughout the HSA molecule, despite its symmetrical repeating domain structure.


==Disease==
==Disease==
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[[Category: plasma protein]]
[[Category: plasma protein]]


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Revision as of 12:55, 21 February 2008

File:1bj5.jpg


1bj5, resolution 2.5Å

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HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID

OverviewOverview

Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has remained elusive. We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar side chains, many of which are basic. These pockets are distributed asymmetrically throughout the HSA molecule, despite its symmetrical repeating domain structure.

DiseaseDisease

Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]

About this StructureAbout this Structure

1BJ5 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites., Curry S, Mandelkow H, Brick P, Franks N, Nat Struct Biol. 1998 Sep;5(9):827-35. PMID:9731778

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