We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

S100 protein

From Proteopedia

Revision as of 11:58, 9 December 2014 by Michal Harel (Talk | contribs)

(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)

Jump to: navigation, search

Template:STRUCTURE 4eto

S100 proteins are calcium-binding proteins (CBP) found in vertebrates and contain 2 helix-loop-helix calcium binding sites. S100 name is derived from their being 100% soluble in ammonium sulfate. There are at least 21 S100 proteins. Most S100 proteins undergo conformational change upon calcium binding.
S100-A1 is a regulator of myocardial contractility.
S100-A2 may have a tumor suppression function.
S100-A4 and S100-A11 may function in motility, invasion and tubulin polymerization.
S100-A6 may function in calcium-dependent insulin release.
S100-A7 is an antimicrobial peptide mainly against E. coli.
S100-A8 combined with S100-A9 (calprotectin) may function in the inhibition of casein kinase and regulate inflammatory processes.
S100-A10 is implicated in the transport of neurotransmitters.
S100-A12 and S100-A13 may function in calcium-dependent signal transduction pathways.
S100-A15 is found in psoriatic skin and functions as antimicrobial peptide.
S100B levels increase in patients suffering from brain damage and are used as diagnostics for traumatic head injury.
S100G is vitamin-D dependent calcium-binding protein and is called calbindin D9k and calbindin D28k depending on its molecular weight. S100G mediates the transport of calcium across enterocytes.