1o9x
From Proteopedia
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HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN
Overview
BACKGROUND: Human serum albumin (HSA) is an abundant plasma protein that, binds a wide variety of hydrophobic ligands including fatty acids, bilirubin, thyroxine and hemin. Although HSA-heme complexes do not bind, oxygen reversibly, it may be possible to develop modified HSA proteins or, heme groups that will confer this ability on the complex. RESULTS: We, present here the crystal structure of a ternary HSA-hemin-myristate, complex, formed at a 1:1:4 molar ratio, that contains a single hemin group, bound to subdomain IB and myristate bound at six sites. The complex, displays a conformation that is intermediate between defatted HSA and, HSA-fatty acid complexes; this is likely to be due to low myristate, occupancy in the fatty acid binding sites that drive the conformational, change. The ... [(full description)]
About this Structure
1O9X is a [Single protein] structure of sequence from [Homo sapiens] with MYR and HEM as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structural analysis of human serum albumin complexed with hemin and fatty acid., Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S, BMC Struct Biol. 2003 Jul 7;3:6. Epub 2003 Jul 7. PMID:12846933
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