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4I2W

Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp70 peptide

Summary for 4I2W
Entry DOI10.2210/pdb4i2w/pdb
Related4I2Z
DescriptorProtein UNC-45, Heat shock 70 kDa protein A (2 entities in total)
Functional Keywordschaperone, 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 sourceCaenorhabditis elegans (nematode)
More
Total number of polymer chains2
Total formula weight109915.09
Authors
Clausen, T.,Gazda, L.,Hellerschmied, D. (deposition date: 2012-11-23, release date: 2013-03-13)
Primary citationGazda, 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: 23332754
DOI: 10.1016/j.cell.2012.12.025
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

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건을2024-04-24부터공개중

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