Protein binding motif
From Wikipedia, the free encyclopedia
Protein binding motif is a short protein sequence motif that interacts with other proteins. A typical example of such motif are proline-rich sequences that are responsible for binding of SH3 domains.
Protein binding sequences may be locally unfolded, as in many endocytic proteins. For example, some EH domains (e.g. in Eps15 protein) contain at least 15 repeats of Asp-Pro-Phe tripeptide, which are responsible for interaction with multiple copies of the AP2 alpha appendage protein.
[edit] External reading
- 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
