2yvc

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[[Image:2yvc.png|left|200px]]
[[Image:2yvc.png|left|200px]]
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==About this Structure==
==About this Structure==
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2YVC is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVC OCA].
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[[2yvc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVC OCA].
==Reference==
==Reference==
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[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:53:58 2009''
 

Revision as of 22:26, 14 March 2011

Template:STRUCTURE 2yvc

Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail

Template:ABSTRACT PUBMED 17459884

About this Structure

2yvc is a 6 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

  • Terawaki S, Kitano K, Hakoshima T. Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex. J Biol Chem. 2007 Jul 6;282(27):19854-62. Epub 2007 Apr 24. PMID:17459884 doi:10.1074/jbc.M609232200
  • Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 2000 Sep 1;19(17):4449-62. PMID:10970839 doi:10.1093/emboj/19.17.4449
  • Hamada K, Shimizu T, Yonemura S, Tsukita S, Tsukita S, Hakoshima T. Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO J. 2003 Feb 3;22(3):502-14. PMID:12554651 doi:10.1093/emboj/cdg039
  • Terawaki S, Maesaki R, Hakoshima T. Structural basis for NHERF recognition by ERM proteins. Structure. 2006 Apr;14(4):777-89. PMID:16615918 doi:10.1016/j.str.2006.01.015

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