2pzo

From Proteopedia

Revision as of 21:21, 12 November 2007

Crystal structure of the zinc-knuckle 2 domain of human CLIP-170 in complex with CAP-Gly domain of human Dynactin-1 (p150-Glued)

Overview

In all eukaryotes, CAP-Gly proteins control important cellular processes., The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed, between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle, of CLIP170 as a model system to explore the structure-function, relationship of CAP-Gly-mediated protein interactions. We demonstrate that, the conserved GKNDG motif of CAP-Gly domains is responsible for targeting, to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and, microtubules. The CAP-Gly-EEY/F interaction is essential for the, recruitment of the dynactin complex by CLIP170 and for activation of, CLIP170. Our findings define the molecular basis of CAP-Gly domain, function, including the tubulin detyrosination-tyrosination cycle. They, further establish fundamental roles for the interaction between CAP-Gly, proteins and C-terminal EEY/F sequence motifs in regulating complex and, dynamic cellular processes.

Disease

Known diseases associated with this structure: Amyotrophic lateral sclerosis, susceptibility to OMIM:[601143], Neuropathy, distal hereditary motor, type VIIB OMIM:[601143]

About this Structure

2PZO is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Structure-function relationship of CAP-Gly domains., Weisbrich A, Honnappa S, Jaussi R, Okhrimenko O, Frey D, Jelesarov I, Akhmanova A, Steinmetz MO, Nat Struct Mol Biol. 2007 Oct;14(10):959-67. Epub 2007 Sep 9. PMID:17828277

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