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FEBS Lett. 2005 Jul 4;579(17):3503-7.

Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins.

Author information

1
Stem Cell Gene Therapy Research Group, Institute of Nuclear Medicine and Allied Sciences, DRDO, Delhi 110054, India. gugdutta@rediffmail.com

Abstract

The sequence of Bcl-2 homology domains, BH1 and BH2, is known to be conserved among anti- and pro-apoptotic members of Bcl-2 family proteins. But structural conservation of these domains with respect to functionally active residues playing role in heterodimerization-mediated regulation of apoptosis has never been elucidated. Here, we have suggested the formation of an active site by structurally conserved residues in BH1 (glycine, arginine) and BH2 (tryptophan) domains of Bcl-2 family members, which also accounts for the functional effect of known mutations in BH1 (G145A, G145E) and BH2 (W188A) domains of Bcl-2.

PMID:
15949801
DOI:
10.1016/j.febslet.2005.05.015
[Indexed for MEDLINE]
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