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1EGX

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

Summary for 1EGX
Entry DOI10.2210/pdb1egx/pdb
Related1evh 1qc6
DescriptorVASODILATOR-STIMULATED PHOSPHOPROTEIN (1 entity in total)
Functional Keywordsevh1, vasp-ena, poly-proline-binding domain, signaling protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P50552
Total number of polymer chains1
Total formula weight12746.36
Authors
Ball, L.,Kuhne, R.,Hoffmann, B.,Hafner, A.,Schmieder, P.,Volkmer-Engert, R.,Hof, M.,Wahl, M.,Schneider-Mergener, J.,Walter, U.,Oschkinat, H.,Jarchau, T. (deposition date: 2000-02-17, release date: 2000-09-20, Last modification date: 2012-07-25)
Primary citationBall, L.J.,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., 19:4903-4914, 2000
Cited by
PubMed: 10990454
DOI: 10.1093/emboj/19.18.4903
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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