1egx: Difference between revisions

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==About this Structure==
==About this Structure==
1EGX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA].  
1EGX is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA].  


==Reference==
==Reference==
Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity., Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T, EMBO J. 2000 Sep 15;19(18):4903-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10990454 10990454]
<ref group="xtra">PMID:10990454</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Ball, L.]]
[[Category: Ball, L.]]
[[Category: Hafner, A.]]
[[Category: Hafner, A.]]
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[[Category: Vasp-ena]]
[[Category: Vasp-ena]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:59:52 2009''

Revision as of 08:59, 18 February 2009

File:1egx.png

Template:STRUCTURE 1egx

SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

Template:ABSTRACT PUBMED 10990454

About this StructureAbout this Structure

1EGX is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

[xtra 1]

  1. Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T. Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. EMBO J. 2000 Sep 15;19(18):4903-14. PMID:10990454 doi:10.1093/emboj/19.18.4903

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