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'''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID''' | '''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID''' | ||
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[[Category: Franks, N.]] | [[Category: Franks, N.]] | ||
[[Category: Mandelkow, H.]] | [[Category: Mandelkow, H.]] | ||
[[Category: | [[Category: Lipid-binding]] | ||
[[Category: | [[Category: Metal-binding]] | ||
[[Category: | [[Category: Plasma protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:35:02 2008'' | |||
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Revision as of 11:35, 2 May 2008
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 disease 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. 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 Page seeded by OCA on Fri May 2 11:35:02 2008