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5NC7

ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2

Summary for 5NC7
Entry DOI10.2210/pdb5nc7/pdb
DescriptorProtein 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 Keywordsproline-rich motif, acta, protein-protein interaction, cell adhesion
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains12
Total formula weight60147.55
Authors
Barone, M.,Roske, Y. (deposition date: 2017-03-03, release date: 2018-03-21, Last modification date: 2024-01-31)
Primary citationBarone, 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: 33184177
DOI: 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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