4I2Z
Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide
Summary for 4I2Z
Entry DOI | 10.2210/pdb4i2z/pdb |
Related | 4I2W |
Descriptor | Protein UNC-45, Heat shock protein 90 (3 entities in total) |
Functional Keywords | chaperone, myosin folding, protein filaments, myofilament formation, tpr-peptide interaction, ucs domain containing protein, hsp70 and hsp90 co-chaperone, chaperone-protein binding complex, chaperone/protein binding |
Biological source | Caenorhabditis elegans (nematode) More |
Cellular location | Cytoplasm, perinuclear region: Q18688 |
Total number of polymer chains | 2 |
Total formula weight | 110109.28 |
Authors | |
Primary citation | Gazda, L.,Pokrzywa, W.,Hellerschmied, D.,Lowe, T.,Forne, I.,Mueller-Planitz, F.,Hoppe, T.,Clausen, T. The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans. Cell(Cambridge,Mass.), 152:183-195, 2013 Cited by PubMed: 23332754DOI: 10.1016/j.cell.2012.12.025 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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