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Atomic structure and chemistry of human serum albumin

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A Corrigendum to this article was published on 22 July 1993

Abstract

The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.

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  1. Daniel C. Carter: To whom correspondence should be addressed.

Authors and Affiliations

  1. The Space Science Laboratory, ES76 Biophysics, Marshall Space Flight Center, Huntsville, Alabama, 35812, USA

    Xiao Min He & Daniel C. Carter

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  1. Xiao Min He
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  2. Daniel C. Carter
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He, X., Carter, D. Atomic structure and chemistry of human serum albumin. Nature 358, 209–215 (1992). https://doi.org/10.1038/358209a0

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