|PROSITE documentation PDOC50105|
The sterile α motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins  involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms . SAM domains have been shown to homo- and hetero-oligomerize , nevertheless with a low-affinity constant , and to mediate specific protein-protein interactions.
Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces [3,4]. In the case of the SAM domain of EphB2, each of these interfaces is able to form dimers . The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures .
Some of the proteins in which such a domain is known to exist are listed below.
We developed a profile that spans the whole domain.Last update:
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Schultz J. Ponting C.P. Hofmann K. Bork P.|
|Title||SAM as a protein interaction domain involved in developmental regulation.|
|Source||Protein Sci. 6:249-253(1997).|
|2||Authors||Stapleton D. Balan I. Pawson T. Sicheri F.|
|Title||The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.|
|Source||Nat. Struct. Biol. 6:44-49(1999).|
|3||Authors||Peterson A.J. Kyba M. Bornemann D. Morgan K. Brock H.W. Simon J.|
|Title||A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions.|
|Source||Mol. Cell. Biol. 17:6683-6692(1997).|
|4||Authors||Thanos C.D. Goodwill K.E. Bowie J.U.|
|Title||Oligomeric structure of the human EphB2 receptor SAM domain.|