5NC7
ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2
Summary for 5NC7
Entry DOI | 10.2210/pdb5nc7/pdb |
Descriptor | Protein enabled homolog, ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization (3 entities in total) |
Functional Keywords | proline-rich motif, acta, protein-protein interaction, cell adhesion |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 12 |
Total formula weight | 60147.55 |
Authors | Barone, M.,Roske, Y. (deposition date: 2017-03-03, release date: 2018-03-21, Last modification date: 2024-01-31) |
Primary citation | Barone, M.,Muller, M.,Chiha, S.,Ren, J.,Albat, D.,Soicke, A.,Dohmen, S.,Klein, M.,Bruns, J.,van Dinther, M.,Opitz, R.,Lindemann, P.,Beerbaum, M.,Motzny, K.,Roske, Y.,Schmieder, P.,Volkmer, R.,Nazare, M.,Heinemann, U.,Oschkinat, H.,Ten Dijke, P.,Schmalz, H.G.,Kuhne, R. Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells. Proc.Natl.Acad.Sci.USA, 117:29684-29690, 2020 Cited by PubMed: 33184177DOI: 10.1073/pnas.2007213117 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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