Arfaptin

Arfaptin
crystal structure analysis of rac1-gdp complexed with arfaptin (p21)
Identifiers
Symbol Arfaptin
Pfam PF06456
Pfam clan CL0145
InterPro IPR010504
SCOP 1i4l

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

  1. ^ 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. 
  2. ^ 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. 

This article incorporates text from the public domain Pfam and InterPro IPR010504