1ckr

HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUESHIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES

Structural highlights 1ckr is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HSP7C_RAT Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540 (18 kDa) and is necessary for the binding of the chaperone with substrate proteins and peptides. The high-resolution NMR solution structure is based on 4150 experimental distance constraints leading to an average root-mean-square precision of 0.38 A for the backbone atoms and 0.76 A for all atoms in the beta-sandwich sub-domain. The protein is observed to bind residue Leu539 in its hydrophobic substrate-binding groove by intramolecular interaction. The position of a helical latch differs dramatically from what is observed in the crystal and solution structures of the homologous prokaryotic chaperone DnaK. In the Hsc70 structure, the helix lies in a hydrophobic groove and is anchored by a buried salt-bridge. Residues involved in this salt-bridge appear to be important for the allosteric functioning of the protein. A mechanism for interdomain allosteric modulation of substrate-binding is proposed. It involves large-scale movements of the helical domain, redefining the location of the hinge area that enables such motions. High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.,Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER J Mol Biol. 1999 Jun 25;289(5):1387-403. PMID:10373374 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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