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Motif domain
From Wikipedia, the free encyclopedia
Motif domains are protein domains that contain periodic short sequence motifs that interact with other proteins. They are in contrast to folded structured domain. For example proline rich domains are motif domain and frequently contain multiple different SH3 binding motifs scattered throughout these relatively unstructured domains. Motif domains are also found in many endocytic proteins, where they again are generally unstructured domains designed to contain a large number of possible protein interaction motifs. For example the motif domain of Eps15 contains at least 15 repeats of DPF and thus can interact with many copies of the AP2 alpha appendage.
Other sequence motifs often fround in motif domains are NPF motifs that bind to EH domains and clathrin terminal domain binding motifs.
- Schmid EM, Ford MG, Burtey A, Praefcke GJ, Peak-Chew SY, Mills IG, Benmerah A, McMahon HT. (2006) Role of the AP2 beta-Appendage Hub in Recruiting Partners for Clathrin-Coated Vesicle Assembly. PLoS Biol. Aug 15;4(9). pubmed
- Praefcke GJ, Ford MG, Schmid EM, Olesen LE, Gallop JL, Peak-Chew SY, Vallis Y, Babu MM, Mills IG, McMahon HT. (2004) Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis. EMBO J. 23, 4371-83. pubmed