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Arfaptin

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Protein domain Protein family
Arfaptin
crystal structure analysis of rac1-gdp complexed with arfaptin (p21)
Identifiers
SymbolArfaptin
PfamPF06456
Pfam clanCL0145
InterProIPR010504
SCOP21i4l / SCOPe / SUPFAM
CDDcd00011
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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. The N-terminal region of ICA69 is similar to arfaptin.

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. S2CID 4324211.
  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 Category:
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