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PROSITE documentation PDOC50105 |
The sterile α motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins [1] involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms [2]. SAM domains have been shown to homo- and hetero-oligomerize [3], nevertheless with a low-affinity constant [4], 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 [4]. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures [4].
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.
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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). | |
PubMed ID | 9007998 |
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). | |
PubMed ID | 9886291 | |
DOI | 10.1038/4917 |
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). | |
PubMed ID | 9343432 |
4 | Authors | Thanos C.D. Goodwill K.E. Bowie J.U. |
Title | Oligomeric structure of the human EphB2 receptor SAM domain. | |
Source | Science 283:833-836(1999). | |
PubMed ID | 9933164 |