Structural similarities between chaperone molecules of the HSP60 and HSP70 families deduced from hydrophobic cluster analysis

FEBS Letters

Burny, Arséne²  Catelli, Maria Grazia¹  Baulieu, Etienne Emile¹  Portetelle, Daniel²  Mornon, Jean Paul³  Callebaut, Isabelle³ 

[1] Unité de Recherches sur les Communications Hormonales, INSERM U33, Hôpital de Bicêtre, 80 rue du Général Leclerc, 94276 Le Kremlin-Bicêtre, France;Faculté des Sciences Agronomiques, 2 passage des Déportés, 5030 Gembloux, Belgium;Département des Macromolécules Biologiques, Laboratoire de Minéralogie-Cristallographie, CNRS URA09, Universités Paris VI-Paris VII, T16, case 115, 4 place Jussieu, 75252 Paris Cedex 05, France

关键词: Hydrophobic cluster analysis;    Heat shock protein;    Molecular chaperone;    Nucleotide binding;    3D;    three-dimensional;    HCA. hydrophobic cluster analysis;    HSP;    heat shock protein;    HSC;    heat shock cognate protein;    MHC;    major histocompatibility complex;    TCP1;    t-complex polypeptide-1;    TF55;    thermophilic factor 55;   

DOI  :  10.1016/0014-5793(94)80510-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this study, the conservation of strong structural landmarks between all the members of two chaperone families (HSP60 and HSP70) was deduced from their sequences by hydrophobic cluster analysis. On this basis, we propose that the ATP-binding environment is maintained by a similar fold in both protein families. The observed similarities extend throughout the proteins, including both the ATPase domain and the C-terminal substrate-binding domain.

【 授权许可】

Unknown