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Atomic structure and chemistry of human serum albuminThe three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. 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 ILIA, 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.
Document ID
19930047631
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
He, Xiao M.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Carter, Daniel C.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 16, 2013
Publication Date
July 16, 1992
Publication Information
Publication: Nature
Volume: 358
Issue: 6383
ISSN: 0028-0836
Subject Category
Life Sciences (General)
Accession Number
93A31628
Distribution Limits
Public
Copyright
Other

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