Interdomain Zinc Site on Human Albumin

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 100; no. 7; pp. 3701 - 3706
• Main Authors: Stewart, Alan J., Blindauer, Claudia A., Berezenko, Stephen, Sleep, Darrell, Sadler, Peter J.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 01.04.2003; National Acad Sciences; The National Academy of Sciences
• Series: Bioinorganic Chemistry Special Feature
• Subjects: Albumins; Amino Acid Substitution; Amino acids; Atoms; Binding Sites; Biochemistry; Bioinorganic Chemistry Special Feature; Calcium - metabolism; Caprylates; Chlorides; Crystallography, X-Ray - methods; Fatty acids; Histidine; Humans; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Physical Sciences; Protein Structure, Secondary; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Serum Albumin - chemistry; Serum Albumin - metabolism; Serum albumins; Zinc; Zinc - chemistry; Zinc - metabolism

Albumin is the major transport protein in blood for Zn2+, a metal ion required for physiological processes and recruited by various drugs and toxins. However, the Zn2+-binding site(s) on albumin is ill-defined. We have analyzed the 18 x-ray crystal structures of human albumin in the PDB and identifi...