1mk7: Difference between revisions

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[[Image:1mk7.gif|left|200px]]
{{Seed}}
[[Image:1mk7.png|left|200px]]


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{{STRUCTURE_1mk7|  PDB=1mk7  |  SCENE=  }}  
{{STRUCTURE_1mk7|  PDB=1mk7  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN CHIMERA'''
===CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN CHIMERA===




==Overview==
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The binding of cytoplasmic proteins, such as talin, to the cytoplasmic domains of integrin adhesion receptors mediates bidirectional signal transduction. Here we report the crystal structure of the principal integrin binding and activating fragment of talin, alone and in complex with fragments of the beta 3 integrin tail. The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors. In combination with NMR and mutational analysis, our studies reveal the critical interacting elements of both talin and the integrin beta 3 tail, providing structural paradigms for integrin linkage to the cell interior.
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{{ABSTRACT_PUBMED_12535520}}


==About this Structure==
==About this Structure==
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[[Category: Npxy motif]]
[[Category: Npxy motif]]
[[Category: Ptb domain]]
[[Category: Ptb domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:16:07 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:09:41 2008''

Revision as of 21:09, 2 July 2008

File:1mk7.png

Template:STRUCTURE 1mk7

CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN CHIMERA

Template:ABSTRACT PUBMED 12535520

About this Structure

1MK7 is a Protein complex structure of sequences from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural determinants of integrin recognition by talin., Garcia-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC, Mol Cell. 2003 Jan;11(1):49-58. PMID:12535520

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