2BUG

Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide

2BUG の概要

• エントリーDOI: 10.2210/pdb2bug/pdb
• 関連するPDBエントリー: 1A17 1S95 1WAO
• NMR情報: BMRB: 6696
• 分子名称: SERINE/THREONINE PROTEIN PHOSPHATASE 5, HSP90 (2 entities in total)
• 機能のキーワード: tetratricopeptide domain, protein phosphatase, hsp90 binding, hydrolase, iron, manganese, metal-binding
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16859.09

構造登録者

Cliff, M.J.,Harris, R.,Barford, D.,Ladbury, J.E.,Williams, M.A. (登録日: 2005-06-13, 公開日: 2006-03-16, 最終更新日: 2024-11-13)

主引用文献

Cliff, M.J.,Harris, R.,Barford, D.,Ladbury, J.E.,Williams, M.A.
Conformational Diversity in the Tpr Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90.
Structure, 14:415-, 2006

PubMed Abstract: Protein phosphatase 5 (Ppp5) is one of several proteins that bind to the Hsp90 chaperone via a tetratricopeptide repeat (TPR) domain. We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90. This structure has the "two-carboxylate clamp" mechanism of peptide binding first seen in the Hop-TPR domain complexes with Hsp90 and Hsp70 peptides. However, NMR data reveal that the Ppp5 clamp is highly dynamic, and that there are multiple modes of peptide binding and mobility throughout the complex. Although this interaction is of very high affinity, relatively few persistent contacts are found between the peptide and the Ppp5-TPR domain, thus explaining its promiscuity in binding both Hsp70 and Hsp90 in vivo. We consider the possible implications of this dynamic structure for the mechanism of relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins.

PubMed: 16531226
DOI: 10.1016/J.STR.2005.12.009

実験手法

SOLUTION NMR