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Structural conservation of residues in BH1 and BH2 domains of Bcl‐2 family proteins
Author(s) -
Gurudutta Gangenahalli U.,
Verma Yogesh Kr,
Singh Vimal Kishor,
Gupta Pallavi,
Raj H.G.,
Sharma R.K.,
Chandra Ramesh
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.015
Subject(s) - conserved sequence , homology (biology) , biology , protein structure , sequence alignment , homology modeling , protein family , peptide sequence , genetics , amino acid , biochemistry , gene , enzyme
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.