Jan 1, 2007

Insilco analysis of functionally important residues in folate receptors

Bioinformation
Kalidoss RamamoorthyRama Shanker Verma

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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Citations

Mentioned in this Paper

Ligand Binding
Folate
Cysteine
Protein Domain
Folic Acid Measurement
Crystal Structure
Ligands Activity
GenBank
Amino Acid [EPC]
Ligands

About this Paper

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