4.6 Article

SAM domains: uniform structure, diversity of function

Journal

TRENDS IN BIOCHEMICAL SCIENCES
Volume 28, Issue 12, Pages 625-628

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2003.11.001

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Funding

  1. NCI NIH HHS [R01 CA081000] Funding Source: Medline
  2. NATIONAL CANCER INSTITUTE [R01CA081000] Funding Source: NIH RePORTER

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Sterile alpha motif (SAM) domains are known to exhibit diverse protein-protein interaction modes. They can form multiple self-association architectures and also bind to various non-SAM domain-containing proteins. Surprising new work adds a completely unanticipated function for some SAM domains - the ability to bind RNA. Such functional diversity within a homologous protein family presents a significant challenge for bioinformatic function assignment.

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