+Search query
-Structure paper
Title | The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans. |
---|---|
Journal, issue, pages | Cell(Cambridge,Mass. ), Vol. 152, Page 183-195, Year 2013 |
Publish date | Nov 23, 2012 (structure data deposition date) |
![]() | Gazda, L. / Pokrzywa, W. / Hellerschmied, D. / Lowe, T. / Forne, I. / Mueller-Planitz, F. / Hoppe, T. / Clausen, T. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.9 - 3.6 Å |
Structure data | ![]() PDB-4i2w: ![]() PDB-4i2z: |
Chemicals | ![]() ChemComp-HOH: |
Source |
|
![]() | Chaperone/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 |