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Structure paper

TitleArrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding.
Journal, issue, pagesJ. Physiol. (Lond. ), Vol. 598, Page 1169-1186, Year 2020
Publish dateAug 21, 2019 (structure data deposition date)
AuthorsWang, K. / Brohus, M. / Holt, C. / Overgaard, M.T. / Wimmer, R. / Van Petegem, F.
External linksJ. Physiol. (Lond. ) / PubMed:32012279
MethodsX-ray diffraction
Resolution1.65 - 2.4 Å
Structure data

PDB-6u39:
2.4 Angstrom crystal structure of the D129G Ca-CaM:CaV1.2 IQ domain complex
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6u3a:
1.65 Angstrom crystal structure of the N97S Ca-CaM:CaV1.2 IQ domain complex
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6u3b:
1.7 Angstrom crystal structure of the Q135P Ca-CaM:CaV1.2 IQ domain complex
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6u3d:
1.75 Angstrom crystal structure of the N53I Ca-CaM:CaV1.2 IQ domain complex
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCALCIUM-BINDING PROTEIN/MEMBRANE PROTEIN / MEMBRANE PROTEIN / CALCIUM-BINDING PROTEIN-MEMBRANE PROTEIN complex / Complex

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