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Title

 

 

 

 

Insilco analysis of functionally important residues in folate receptors

 

Authors

Kalidoss Ramamoorthy1, Sirisha Potala1 and Rama Shanker Verma1, *

 

Affiliation

1Department of Biotechnology, Indian Institute of Technology Madras, Chennai-600036, TN, India

 

Phone

091 44 2257 4109

 

Fax

091 44 2257 4102

 

Email

vermars@iitm.ac.in; * Corresponding author

 

Article Type

Hypothesis

 

Date

received November 15, 2007; revised November 23, 2007; accepted December 11, 2007; published online December 28, 2007

 

Abstract

Lack of crystal structure data of folate binding proteins has left so many questions unanswered (for example, important residues in active site, binding domain, important amino acid residues involved in interactions between ligand and receptor). With sequence alignment and PROSITE motif identification, we attempted to answer evolutionarily significant residues that are of functional importance for ligand binding and that form catalytic sites.  We have analyzed 46 different FRs and FBP sequences of various organisms obtained from Genbank.  Multiple sequence alignment identified 44 highly conserved identical amino acid residues with 10 cysteine residues and 12 motifs including ECSPNLGPW (which might help in the structural stability of FR).

 

Keywords

folate receptors (FR); folate binding proteins (FBP); multiple sequence alignment; consensus sequence; conserved motifs; evolutionary trace (ET)

 

Citation

Ramamoorthy et al., Bioinformation 2(4): 157-162 (2007)

 

Edited by

P. Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.