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TitleThe IQGAP1 N-Terminus Forms Dimers, and the Dimer Interface Is Required for Binding F-Actin and Calcium-Bound Calmodulin.
Journal, issue, pagesBiochemistry, Vol. 55, Page 6433-6444, Year 2016
Publish dateJul 7, 2009 (structure data deposition date)
AuthorsLiu, J. / Kurella, V.B. / LeCour Jr., L. / Vanagunas, T. / Worthylake, D.K.
External linksBiochemistry / PubMed:27798963
MethodsX-ray diffraction
Resolution2.36 - 2.5 Å
Structure data

PDB-3i6x:
Crystal structure of the calponin homology domain of IQGAP1
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5l0o:
IQGAP1 calponin homology domain fragment (CHDF) mutant K161C under oxidizing conditions
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCALMODULIN-BINDING / MEMBRANE PROTEIN / all Helical / Cell membrane / Membrane / Phosphoprotein / PROTEIN BINDING / SIGNALING PROTEIN / Calponin homology / disulfide-bonded dimer

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