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Structure paper

TitleStructural Analysis of the Interactions between Paxillin Ld Motifs and Alpha-Parvin
Journal, issue, pagesStructure, Vol. 16, Page 1521-, Year 2008
Publish dateJul 31, 2008 (structure data deposition date)
AuthorsLorenz, S. / Vakonakis, I. / Lowe, E.D. / Campbell, I.D. / Noble, M.E.M. / Hoellerer, M.K.
External linksStructure / PubMed:18940607
MethodsX-ray diffraction
Resolution1.05 - 2.2 Å
Structure data

PDB-2vzc:
Crystal structure of the C-terminal calponin homology domain of alpha parvin
Method: X-RAY DIFFRACTION / Resolution: 1.05 Å

PDB-2vzd:
Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex with paxillin LD1 motif
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2vzg:
Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD2 motif
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2vzi:
Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD4 motif
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-GOL:
GLYCEROL

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
KeywordsCELL ADHESION / MEMBRANE / CYTOPLASM / CYTOSKELETON / CELL JUNCTION / ALTERNATIVE SPLICING / CALPONIN HOMOLOGY DOMAIN / ACTIN-BINDING / CELL MEMBRANE / METAL-BINDING / PHOSPHOPROTEIN / LD1 MOTIF / LIM DOMAIN / LD2 MOTIF

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