1pls
From Proteopedia
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'''SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN''' | '''SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN''' | ||
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[[Category: Petros, A M.]] | [[Category: Petros, A M.]] | ||
[[Category: Yoon, H S.]] | [[Category: Yoon, H S.]] | ||
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Revision as of 02:13, 3 May 2008
SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN
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.
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 Sat May 3 05:13:53 2008
