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TitleThe myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 152, Page 183-195, Year 2013
Publish dateNov 23, 2012 (structure data deposition date)
AuthorsGazda, L. / Pokrzywa, W. / Hellerschmied, D. / Lowe, T. / Forne, I. / Mueller-Planitz, F. / Hoppe, T. / Clausen, T.
External linksCell(Cambridge,Mass. ) / PubMed:23332754
MethodsX-ray diffraction
Resolution2.9 - 3.6 Å
Structure data

PDB-4i2w:
Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp70 peptide
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-4i2z:
Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • caenorhabditis elegans (invertebrata)
KeywordsChaperone/protein binding / chaperone / myosin folding / protein filaments / myofilament formation / TPR-peptide interaction / UCS domain containing protein / Hsp70 and Hsp90 co-chaperone / Chaperone-protein binding complex

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