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Title |
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Insilco analysis of functionally important residues in folate receptors
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Authors |
Kalidoss Ramamoorthy1, Sirisha Potala1 and Rama Shanker Verma1, *
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Affiliation |
1Department of Biotechnology, Indian Institute of Technology Madras, Chennai-600036, TN, India
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| Phone |
091 44 2257 4109
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091 44 2257 4102
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vermars@iitm.ac.in; * Corresponding author
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Article Type |
Hypothesis
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Date |
received November 15, 2007; revised November 23, 2007; accepted December 11, 2007; published online December 28, 2007
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| 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).
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| Keywords |
folate receptors (FR); folate binding proteins (FBP); multiple sequence alignment; consensus sequence; conserved motifs; evolutionary trace (ET) |
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Citation |
Ramamoorthy et al., Bioinformation 2(4): 157-162 (2007)
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Edited by |
P. Kangueane
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ISSN |
0973-2063
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Publisher |
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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. |