|PROSITE documentation PDOC00348 [for PROSITE entry PS50287]|
The scavenger receptor cysteine-rich (SRCR) domain is an ancient and highly conserved domain of about 110 residues which is found in diverse secreted and cell-surface proteins, like the type I scavenger receptor, the speract receptor, CD5/Ly-1, CD6, or complement factor I . Tandem repeats of SRCR domains are common in the membrane bound proteins. Most SRCR domains have six to eight cysteines that participate in intradomain disulfide bonds. SRCR domains have been subdivided into two groups, A and B, primarily on the differences in the spacing pattern between the cysteine residues [2,3].
Determination of the crystal structure of the SRCR domain of M2BP reveals that the M2NP SRCR adopts a compact fold of approximate dimensions 22 x 26 x 30 Angstrom, organized around a curved six-stranded β-sheet cradling an α-helix .
Some proteins known to contain one or more SRCR domains are listed below:
The signature pattern that we derived spans part of the N-terminal section of the domain and contain 8 conserved residues. The profile spans the complete domain.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Freeman M. Ashkenas J. Rees D.J. Kingsley D.M. Copeland N.G. Jenkins N.A. Krieger M.|
|Title||An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 87:8810-8814(1990).|
|2||Authors||Resnick D. Pearson A. Krieger M.|
|Title||The SRCR superfamily: a family reminiscent of the Ig superfamily.|
|Source||Trends Biochem. Sci. 19:5-8(1994).|
|3||Authors||Hohenester E. Sasaki T. Timpl R.|
|Title||Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.|
|Source||Nat. Struct. Biol. 6:228-232(1999).|