401. Fold prediction and comparative modeling of Bdm1: a probable alpha/beta hydrolase associated with hot water epilepsy.
- Author
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Bhaduri A, Krishnaswamy L, Ullal GR, Panicker MM, and Sowdhamini R
- Subjects
- Amino Acid Sequence, Animals, Binding Sites, Catalytic Domain genetics, Epilepsy, Reflex enzymology, Epilepsy, Reflex genetics, Humans, Hydrolases genetics, Hydrolases metabolism, Hydrolysis, Models, Molecular, Molecular Sequence Data, Muscle Proteins genetics, Muscle Proteins metabolism, Nerve Tissue Proteins genetics, Nerve Tissue Proteins metabolism, Protein Conformation, Rats, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity, Hydrolases chemistry, Muscle Proteins chemistry, Nerve Tissue Proteins chemistry, Protein Folding
- Abstract
Hot water epilepsy (HWE) is a benign and rare form of reflex epilepsy that occurs most commonly in humans. Bdm1 is one of the proteins whose mRNA transcript is overexpressed during HWE in a rat model. We show, by sequence analysis and fold recognition methods, that Bdm1 has strong structural similarities to alpha/beta hydrolases like the thioesterases. A three-dimensional model derived by comparative modeling methods allowed the search for catalytic residues using a flexible functional template characteristic of these enzymes. We predict that Bdm1 might be regulated by homocysteine levels by means of direct participation in degradation pathways.
- Published
- 2003
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