Methotrexate: Difference between revisions

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Joel L. Sussman (talk | contribs)
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== Structural Features DHFR==
== Structural Features DHFR==


Human DHFR can be visualized 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>.
Human DHFR can be visualized 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='42/420816/Secondary_structure_2w3m/10'>Text To Be Displayed</scene>
 
<scene name='42/420816/Secondary_structure_2w3m/10'>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>.
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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