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Protein Engineering, Vol. 12, No. 6, 439-446, June 1999
© 1999 Oxford University Press

Crystal structure of human serum albumin at 2.5 Å resolution

S. Sugio1, A. Kashima, S. Mochizuki, M. Noda and K. Kobayashi2

Osaka Laboratories, Yoshitomi Pharmaceutical Industries Ltd,2-25-1, Shodai-Ohtani, Hirakata, Osaka 573-1153, Japan

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 C{alpha} atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the C{alpha} 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.

Keywords: crystal structure/human serum albumin/recombinant protein

1 Present address: Mitsubishi Chemical Corporation, Yokohama 227-8502, Japan

2 To whom all correspondence should be addressed


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