1CKR

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

1CKR の概要

• エントリーDOI: 10.2210/pdb1ckr/pdb
• 分子名称: HEAT SHOCK SUBSTRATE BINDING DOMAIN OF HSC-70 (1 entity in total)
• 機能のキーワード: molecular chaperone, hsp70, peptide binding, protein folding, chaperone
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17558.75

構造登録者

Morshauser, R.C.,Hu, W.,Wang, H.,Pang, Y.,Flynn, G.C.,Zuiderweg, E.R.P. (登録日: 1999-04-22, 公開日: 1999-04-30, 最終更新日: 2023-12-27)

主引用文献

Morshauser, R.C.,Hu, W.,Wang, H.,Pang, Y.,Flynn, G.C.,Zuiderweg, E.R.
High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.
J.Mol.Biol., 289:1387-1403, 1999

PubMed Abstract: 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.

PubMed: 10373374
DOI: 10.1006/jmbi.1999.2776

実験手法

SOLUTION NMR