Methotrexate: Difference between revisions

Human DHFR can be visualized as an <scene name='Sandbox_58/Asymmetric_unit/1'>asymmetric unit</scene> as well as its <scene name='Sandbox_58/Biological_unit/1'>biological unit</scene>. DHFR contains 4 alpha helical regions and 8 beta sheets as can be seen in its <scene name='Sandbox_58/Secondary_structure_2w3m/1'>secondary structure</scene>. The <scene name='Sandbox_58/Acidic_basic/1'>acidic and basic residues</scene> can also be seen.  Human DHFR catalyzes the reduction of dihydrofolic acid to tetrahydrofolic acid, with NADPH serving as the electron donor in this reaction.  The <scene name='Sandbox_58/Active_site_2w3m-/1'>active site</scene> can be seen with the residues that facilitate substrate binding and reaction process.  The red residues represent the active site amino acid side chains interacting with the substrate, and the blue amino acid side chains help bind NADPH, with both folate and NADPH represented in white.  <scene name='Sandbox_58/Active_site_2w3m-/2'>NADPH and folate</scene> can both be seen interacting with the DHFR enzyme (folate surrounded by red sidechains, and NADPH surrounded by blue sidechains)<ref>Schnell JR, Dyson HJ, Wright PE (June 2004). "Structure, dynamics, and catalytic function of dihydrofolate reductase.". Annual Review of Biophysics and Biomolecular Structure 33: 119–40</ref>.

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<scene name='Sandbox_58/Relative_temperature/1'>relative temperature</scene> are color depictions of each atom in regards to mobility or position uncertainty relative to the molecule, with increasing mobility as the color scheme goes from blue to red.  The interactions of the rest of the protein are depicted through the <scene name='Sandbox_58/H_bonds/1'>hydrogen bonds</scene> displayed in red<ref>Matthews DA, Alden RA, Bolin JT, Freer ST, Hamlin R, Xuong N, Kraut J, Poe M, Williams M, Hoogsteen K (July 1977). "Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate". Science 197 (4302): 452–455.</ref>.  

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