 GRIP Domain | |
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Structure:
 The 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.
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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.
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Examples of Proteins:
| GRIP domain proteins |
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Binding partners |
| Golgins |  |
Arls
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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