Serum albumin family | |||||||||
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Structure of serum albumin.
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Identifiers | |||||||||
Symbol | Serum_albumin | ||||||||
Pfam | PF00273 | ||||||||
Pfam clan | CL0282 | ||||||||
InterPro | IPR014760 | ||||||||
SMART | SM00103 | ||||||||
PROSITE | PS51438 | ||||||||
SCOP | 1ao6 | ||||||||
SUPERFAMILY | 1ao6 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
The albumins (formed from Latin: albumen "(egg) white; dried egg white") are a family of globular proteins, the most common of which are the serum albumins. All the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated. Substances containing albumins, such as egg white, are called albuminoids.
A number of blood transport proteins are evolutionarily related, including serum albumin, alpha-fetoprotein, vitamin D-binding protein and afamin.
Albumin binds to the cell surface receptor albondin.
Serum albumin is the main protein of human blood plasma. It binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin, thyroxine (T4) and pharmaceuticals (including barbiturates): its main function is to regulate the Oncotic pressure of blood. Alpha-fetoprotein (alpha-fetoglobulin) is a fetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. The isoelectric point of albumin is 4.9.
The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ångströms (250 pm). Albumin is a 65–70 kDa protein.