Protein binding motif

You don't need to be Editor-In-Chief to add or edit content to WikiDoc. You can begin to add to or edit text on this WikiDoc page by clicking on the edit button at the top of this page. Next enter or edit the information that you would like to appear here. Once you are done editing, scroll down and click the Save page button at the bottom of the page.

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.

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