1upt

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 1upt Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.70Å
Sites:
Ligands:	and
Coordinates:	save as pdb, mmCIF, xml

STRUCTURE OF A COMPLEX OF THE GOLGIN-245 GRIP DOMAIN WITH ARL1

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Golgins are large coiled-coil proteins that play a role in Golgi structure and vesicle traffic. The Arf-like GTPase Arl1 regulates the translocation of GRIP domain-containing golgins to Golgi membranes. We report here the 1.7 A resolution structure of human Arl1-GTP in a complex with the GRIP domain of golgin-245. The structure reveals that the GRIP domain consists of an S-shaped arrangement of three helices. The domain forms a homodimer that binds two Arl1-GTPs using two helices from each monomer. The structure is consistent with golgin-245 forming parallel coiled-coils and suggests how Arl1-GTP/GRIP complexes interact with Golgi membranes via the N termini of Arl1-GTP and the C-terminal tails of the GRIP domains. In cells, bivalent association with Arl1-GTP would increase residence time of the golgins on Golgi membranes. Despite no conservation of sequence, topology, or even helical direction, several other effectors form similar interactions with small GTPases via a pair of alpha helices, suggesting a common structural basis for effector recognition.

Disease

Known disease associated with this structure: Leukemia, chronic lymphatic, susceptibility to OMIM:[609351]

About this Structure

1UPT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus., Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S, Mol Cell. 2003 Oct;12(4):863-74. PMID:14580338

Page seeded by OCA on Sun Mar 23 13:53:58 2008