1pls
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1pls" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pls" /> '''SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY...)
Next diff →
Revision as of 16:38, 12 November 2007
|
SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN
Contents |
Overview
Pleckstrin, the major protein kinase C substrate of platelets, contains, domains of about 100 amino acids at the amino and carboxy termini that, have been found in a number of proteins, including serine/threonine, kinases, GTPase-activating proteins, phospholipases and cytoskeletal, proteins. These conserved sequences, termed pleckstrin-homology (PH), domains, are thought to be involved in signal transduction. But the, details of the function and binding partners of the PH domains have not, been characterized. Here we report the solution structure of the, N-terminal pleckstrin-homology domain of pleckstrin determined using, heteronuclear three-dimensional nuclear magnetic resonance spectroscopy., The structure consists of an up-and-down beta-barrel of seven antiparallel, beta-strands and a C-terminal amphiphilic alpha-helix that caps one end of, the barrel. The overall topology of the domain is similar to that of the, retinol-binding protein family of structures.
Disease
Known disease associated with this structure: Age-related maculopathy, susceptibility to OMIM:[607772]
About this Structure
1PLS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a pleckstrin-homology domain., Yoon HS, Hajduk PJ, Petros AM, Olejniczak ET, Meadows RP, Fesik SW, Nature. 1994 Jun 23;369(6482):672-5. PMID:8208296
Page seeded by OCA on Mon Nov 12 18:45:05 2007
