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]
| 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 | ||||||||
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References
edit- ^ 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.