1dyn
From Proteopedia
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'''CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN''' | '''CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN''' | ||
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[[Category: Schlessinger, J.]] | [[Category: Schlessinger, J.]] | ||
[[Category: Sigler, P B.]] | [[Category: Sigler, P B.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:26:23 2008'' | |
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Revision as of 11:26, 2 May 2008
CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN
Overview
The X-ray crystal structure of the pleckstrin homology (PH) domain from human dynamin has been refined to 2.2 A resolution. A seven-stranded beta sandwich of two orthogonal antiparallel beta sheets is closed at one corner by a C-terminal alpha helix. Opposite this helix are the three loops that vary most among PH domains. The basic fold is very similar to that of two other PH domains recently determined by nuclear magnetic resonance, confirming that PH domain with known structure is electrostatically polarized, with the three variable loops forming a positively charged surface. This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface.
About this Structure
1DYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1994 Oct 21;79(2):199-209. PMID:7954789 Page seeded by OCA on Fri May 2 14:26:23 2008
