| Arfaptin | |||||||
|---|---|---|---|---|---|---|---|
 crystal structure analysis of rac1-gdp complexed with arfaptin (p21) | |||||||
| Identifiers | |||||||
| Symbol | Arfaptin | ||||||
| Pfam | PF06456 | ||||||
| Pfam clan | CL0145 | ||||||
| InterPro | IPR010504 | ||||||
| SCOP2 | 1i4l / SCOPe / SUPFAM | ||||||
| CDD | cd00011 | ||||||
| |||||||
In molecular biology, the arfaptin domain is a protein domain which interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils.1 The N-terminal region of ICA69 is similar to arfaptin.2
References
References
- Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ (May 2001). "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways". Nature. 411 (6834): 215–9. doi:10.1038/35075620. PMID 11346801. S2CID 4324211.
- Spitzenberger F, Pietropaolo S, Verkade P, Habermann B, Lacas-Gervais S, Mziaut H, Pietropaolo M, Solimena M (July 2003). "Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells". J. Biol. Chem. 278 (28): 26166–73. doi:10.1074/jbc.M213222200. PMID 12682071.