2dyn

From Proteopedia

Revision as of 19:34, 12 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

2dyn, resolution 2.30Å

Drag the structure with the mouse to rotate

DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)

Contents

Overview

The pleckstrin homology (PH) domain is a conserved module present in many, signal transducing and cytoskeletal proteins. Here we report the 2.8 A, crystal structure of the PH domain from dynamin. This domain consists of, seven beta-strands forming two roughly orthogonal antiparallel beta-sheets, terminating with an amphipathic alpha-helix. The structure also reveals a, non-covalent dimeric association of the PH domain and a hydrophobic pocket, surrounded by a charged rim. The dynamin PH domain structure is discussed, in relation to its potential role in mediating interactions between, proteins.

Disease

Known diseases associated with this structure: Charcot-Marie-Tooth disease, dominant intermediate B OMIM:[602378], Myopathy, centronuclear OMIM:[602378]

About this Structure

2DYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the pleckstrin homology domain from dynamin., Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T, Nat Struct Biol. 1994 Nov;1(11):782-8. PMID:7634088

Page seeded by OCA on Mon Nov 12 21:40:58 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools