Article
Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation.
Biochemistry - 18 Apr 2006
Pejchal Robert, Campbell Elizabeth, Guenther Brian D, Lennon Brett W, Matthews Rowena G, Ludwig Martha L
Abstract excerpt
In human methylenetetrahydrofolate reductase (MTHFR) the Ala222Val (677C-->T) polymorphism encodes a heat-labile gene product that is associated with elevated levels of homocysteine and possibly with risk for cardiovascular disease. Generation of the equivalent Ala to Val mutation in Escherichia coli MTHFR, which is 30% identical to the catalytic domain of the human enzyme, creates a protein with enhanced...
Topics
- Alanine
- Amino Acid Sequence
- Binding Sites
- Crystallography, X-Ray
- Enzyme Activation
- Escherichia coli
- Flavin-Adenine Dinucleotide
- Folic Acid
- Humans
- Ligands
- Methylenetetrahydrofolate Reductase (NADPH2)
- Models, Molecular
- Molecular Sequence Data