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TitlePharmacological inhibition of syntenin PDZ2 domain impairs breast cancer cell activities and exosome loadifing with syndecan and EpCAM cargo.
Journal, issue, pagesJ Extracell Vesicles, Vol. 10, Page e12039-e12039, Year 2020
Publish dateApr 3, 2019 (structure data deposition date)
AuthorsLeblanc, R. / Kashyap, R. / Barral, K. / Egea-Jimenez, A.L. / Kovalskyy, D. / Feracci, M. / Garcia, M. / Derviaux, C. / Betzi, S. / Ghossoub, R. ...Leblanc, R. / Kashyap, R. / Barral, K. / Egea-Jimenez, A.L. / Kovalskyy, D. / Feracci, M. / Garcia, M. / Derviaux, C. / Betzi, S. / Ghossoub, R. / Platonov, M. / Roche, P. / Morelli, X. / Hoffer, L. / Zimmermann, P.
External linksJ Extracell Vesicles / PubMed:33343836
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-6r9h:
Crystal structure of the PDZ tandem of syntenin in complex with fragment C58
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6rlc:
Crystal structure of the PDZ tandem of syntenin in complex with fragment F13
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-JVK:
(2~{S})-2-[2-(4-chlorophenyl)sulfanylethanoylamino]-3-methyl-butanoic acid

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-K7Z:
(2~{S})-2-[3-(4-chlorophenyl)sulfanylpropanoylamino]-3-methyl-butanoic acid

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / signaling protein cell adhesion PDZ domain syntenin syndecan drug design

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