TY  - JOUR
ID  - open176
UR  - http://www.benthamdirect.org/pages/content.php?CPPS/2005/00000006/00000002/0003K.SGM
IS  - 2
A1  - Kishan, K V Radha
A1  - Agrawal, Vishal
N2  - The folding space for all the protein sequences is limited. Therefore it was observed that many proteins, whose sequences are not related, have similar fold characteristics. The fold databases like SCOP and CATH have classified various protein folds. However, in-depth analysis of the functional features of these folds was not done. We analyzed about twenty unique SH3-like folded proteins in their structural environment and functional characteristics. From our analysis it is apparent that the SH3-like folds could carry out various functions by modulation of loops and the functional region is restricted to one side of a particular sheet helped by two or three loops. The functions vary from oligonucleotide-binding to peptide-binding and other ligand binding. Although certain degree of sequence similarity was observed among the SH3-fold proteins, the similarity was restricted to the beta-strand regions of the proteins.
VL  - 6
TI  - SH3-like fold proteins are structurally conserved and functionally divergent.
AV  - none
EP  - 50
N1  - Copyright of this article belongs to Bentham Science.
Y1  - 2005/04//
PB  - Bentham Science
JF  - Current protein & peptide science
KW  - src homology
KW  -  motif binding
KW  -  tim-barrel fold
KW  -  dna-binding (hid) domain
KW  -  hidden
KW  -  markov model (hmm)
KW  -  dihydrofolate reductase (dhfr) 
SN  - 1389-2037
SP  - 143
ER  -