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Volume 579, Issue 17, Pages 3503-3507 (4 July 2005)


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

Edited by Gianni Cesareni

Gangenahalli U. GuruduttaacCorresponding Author Information1email address, Yogesh Kr Vermaa1, Vimal Kishor Singha, Pallavi Guptaa, H.G. Rajd, R.K. Sharmab, Ramesh Chandrae

Received 3 March 2005; received in revised form 25 April 2005; accepted 25 April 2005. published online 01 June 2005.

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.

a Stem Cell Gene Therapy Research Group, Institute of Nuclear Medicine and Allied Sciences, DRDO, Delhi 110054, India

b Division of Radiopharmaceuticals, Institute of Nuclear Medicine and Allied Sciences, DRDO, Delhi 110054, India

c Department of Hematology, School of Medicine, Hematology/Oncology and Stem Cell Therapeutics Division, University of Pennsylvania, BRB II/III, Room Number 727, UPENN, 421, Curie Boulevard, Philadelphia, PA 19104, USA

d Department of Biochemistry, VP Chest Institute, Delhi 7, India

e Dr. B.R. Ambedkar Centre for Biomedical Research, University of Delhi, Mall Road, Delhi, India

Corresponding Author InformationCorresponding author. Fax: +1 215 573 7049.

1 Authors contributed equally.

PII: S0014-5793(05)00613-7

doi:10.1016/j.febslet.2005.05.015


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