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GRIP Domain

No ImageThe structure shown is the crystal structure of the GRIP domain from golgin-245 in complex with Arl1-GTP, a member of the ARF/Arl small GTPase family. The interaction is predominantly mediated through hydrophobic interactions with the switch II region of Arl1. The GRIP domain also forms a tight homodimer whereby each subunit interacts independently with one Arl1-GTP; such dimerization appears to be required for GRIP domain-mediated Golgi targeting. 

Structure Reference:

Panic, B. et al. (2003) Mol. Cell. 12(4): 863-874. PDB: 1UPT.

Domain binding and function:
The GRIP domain was originally identified as a conserved C-terminal domain present in a group of Golgi proteins from yeast and mammals. It was subsequently shown that GRIP interacted with the Arf/Ar1 family of small GTPases, Arl1 and Arl3. The GRIP domain structure consists of an S-shaped configuration of three helices with a concave and a convex face. The domain can form a head to tail homodimer that allow for Arl1-GTP proteins to interact. It is suggested that this domain may be a conserved device among eukaryotes that are involved in Golgi targeting.
Examples of Proteins: 
GRIP domain proteins
Binding partners
Golgins Arls

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