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Structure paper

TitleThe structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics.
Journal, issue, pagesStructure, Vol. 21, Page 342-354, Year 2013
Publish dateAug 30, 2012 (structure data deposition date)
AuthorsLiu, X. / Shepherd, T.R. / Murray, A.M. / Xu, Z. / Fuentes, E.J.
External linksStructure / PubMed:23395182
MethodsX-ray diffraction
Resolution1.54 - 1.85 Å
Structure data

PDB-4gvc:
Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with phosphorylated Syndecan1 Peptide
Method: X-RAY DIFFRACTION / Resolution: 1.54 Å

PDB-4gvd:
Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with Syndecan1 Peptide
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-ANS:
5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID)

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / phosphorylation / peptide conformational change / new binding pocket / scaffold signaling protein for cell adhesion and cell junction / syndecan1 P1 Tyr phosphorylation / sydencan1 N-terminal Thr dansylation / conformational change during phosphorylation / different binding pocket from phosphorylated sydencan1

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