1mi1

From Proteopedia

---

Revision as of 16:05, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1mi1, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

Overview

The BEACH domain is highly conserved in a large family of eukaryotic, proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any, sequence homology with other proteins. Here we report the crystal, structure at 2.9 A resolution of the BEACH domain of human neurobeachin., It shows that the BEACH domain has a new and unusual polypeptide backbone, fold, as the peptide segments in its core do not assume regular secondary, structures. Unexpectedly, the structure also reveals that the BEACH domain, is in extensive association with a novel, weakly conserved, pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong, interactions, suggesting they may function as a single unit. Functional, studies in intact cells demonstrate the requirement of both the PH and the, BEACH domains for activity. A prominent groove at the interface between, the two domains may be used to recruit their binding partners.

About this Structure

1MI1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain., Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L, EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919

Page seeded by OCA on Mon Nov 12 18:11:39 2007