Arfaptin Explained
| Symbol: | Arfaptin |
| Arfaptin |
| Pfam: | PF06456 |
| Pfam Clan: | CL0145 |
| Interpro: | IPR010504 |
| Scop: | 1i4l |
| 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]
Notes and References
- Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ . The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways . Nature . 411 . 6834 . 215–9 . May 2001 . 11346801 . 10.1038/35075620 . 4324211 .
- Spitzenberger F, Pietropaolo S, Verkade P, Habermann B, Lacas-Gervais S, Mziaut H, Pietropaolo M, Solimena M . 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 . July 2003 . 12682071 . 10.1074/jbc.M213222200 . free .
