Format

Send to

Choose Destination
FEBS Lett. 2002 Oct 9;529(2-3):162-7.

p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families.

Author information

1
Protein Design Group, Centro Nacional de Biotecnologia, 28049 Cantoblanco, Madrid, Spain. garcia@gredos.cnb.uam.es

Abstract

We identified families of proteins characterized by the presence of a domain similar to human p23 protein, which include proteins such as Sgt1, involved in the yeast kinetochore assembly; melusin, involved in specific interactions with the cytoplasmic integrin beta1 domain; Rar1, related to pathogenic resistance in plants, and to development in animals; B5+B5R flavo-hemo cytochrome NAD(P)H oxidoreductase type B in humans and mice; and NudC, involved in nucleus migration during mitosis. We also found that p23 and the HSP20/alpha-crystallin family of heat shock proteins, which share the same three-dimensional folding, show a pattern of conserved residues that points to a common origin in the evolution of both protein domains. The p23 and HSP20/alpha-crystallin phylogenetic relationship and their similar role in chaperone activity suggest a common function, probably involving protein-protein interaction, for those proteins containing p23-like domains.

PMID:
12372593
DOI:
10.1016/s0014-5793(02)03321-5
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center