Seroatlas · Protein domains

Sterile alpha motif domain

IPR001660

Definition

The sterile alpha motif (SAM) domain is a protein interaction module present in a wide variety of proteins [[cite:PMID:9007998], [cite:PMID:21805519]] involved in many biological processes. The SAM domain that spreads over around 70 residues and one of the most common protein modules found in eukaryotic genomes PMID:9886291. SAM domains have been shown to form homo- and hetero-oligomers, forming multiple self-association architectures and also binding to various non-SAM domain-containing proteins PMID:9343432, nevertheless with a low affinity constant PMID:9933164. SAM domains also appear to possess the ability to bind RNA PMID:14659692. Smaug, a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA, binds to the 3' untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain, which could be the RNA-binding surface. This electropositive potential is unique among all previously determined SAM-domain structures and is conserved among Smaug-SAM homologues. These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces PMID:9343432. 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 PMID:9933164.

94 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

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