The complete primary structure of rat chaperonin-10 reveals a putative-beta-alpha-beta nucleotide-binding domain with homology to P21(ras)

Hartman, Dallas J., Hoogenraad, Nicholas J., Condron, Rosemary and Høj, Peter Bordier (1993) The complete primary structure of rat chaperonin-10 reveals a putative-beta-alpha-beta nucleotide-binding domain with homology to P21(ras). Biochimica Et Biophysica Acta, 1164 2: 219-222. doi:10.1016/0167-4838(93)90251-L


Author Hartman, Dallas J.
Hoogenraad, Nicholas J.
Condron, Rosemary
Høj, Peter Bordier
Title The complete primary structure of rat chaperonin-10 reveals a putative-beta-alpha-beta nucleotide-binding domain with homology to P21(ras)
Formatted title
The complete primary structure of rat chaperonin-10 reveals a putative βαβ nucleotide-binding domain with homology to P21ras
Journal name Biochimica Et Biophysica Acta   Check publisher's open access policy
ISSN 0006-3002
Publication date 1993-07-10
Sub-type Other
DOI 10.1016/0167-4838(93)90251-L
Open Access Status Not Open Access
Volume 1164
Issue 2
Start page 219
End page 222
Total pages 4
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Abstract The first complete amino-acid sequence of a mitochondrial chaperonin 10 is reported. The amino-terminal alanine residue is acetylated, a modification that may be required for the interaction with heptameric chaperonin 60. Part of the sequence constitutes a potential dinucleotide binding motif and is identical with 7 out of 10 residues in the GTP-binding site of p21ras. This similarity may be the structural basis for the recently discovered complex between p21ras and chaperonin 60 in intact cells
Keyword Nucleotide binding sequence
Chaperonin
Amino acid sequence
Rat
Q-Index Code CX
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Other
Collection: Office of the Vice-Chancellor
 
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