Publisher Summary This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin. The most outstanding property of albumin is its ability to bind reversibly an incredible variety of ligands. The sequences of all albumins are characterized by a unique arrangement of disulfide double loops that repeat as a series of triplets. Albumin belongs to a multigene family of proteins that includes α- fetoprotein (AFP) and vitamin D-binding protein (VDP), also known as G complement (Gc) protein. Although AFP is considered the fetal counterpart of albumin, its binding properties are distinct and it is suggested that AFP may have a higher affinity for some unknown ligands important for fetal development. Domain structure and the arrangement of the disulfides, the surface charge distribution, and the conformational flexibility of the albumin molecule are described. The nature of ligand binding, including small organics, long-chain fatty acids, and metals, to multiple sites on the albumin molecule is clearly depicted. The chapter concludes with the perceptive comments on future directions being taken to explore the structure and function of this fascinating protein.

Structure of serum albumin.

Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)

The role of oxidized lipoproteins in atherogenesis

Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins

http://www.jbc.org/content/274/41/29303.full.pdf

The Three Recombinant Domains of Human Serum Albumin STRUCTURAL CHARACTERIZATION AND LIGAND BINDING PROPERTIES

http://www.jbc.org/content/242/7/1574.full.pdf

Frank A. Blumenstock

Papers

Copper-binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment