Crystal structure of human serum albumin at 2.5 Å resolution

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ID: 291556
1999
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Abstract
A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 Å resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m.s. deviation of 0.24 Å for all Cα atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Cα atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 Å in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.
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Authors Shigetoshi Sugio, Akiko Kashima, Shota Mochizuki, Masafumi Noda, Kaoru Kobayashi
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Journal Protein Engineering Design and Selection
Year 1999
DOI
10.1093/protein/12.6.439
URL
https://doi.org/10.1093/protein/12.6.439
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