Methotrexate: Difference between revisions

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The nature of this binding has a 1000 fold increase in affinity relative to the natural folate affinity of DHFR , producing a practically irreversible inhibition of DHFR activity. Methotrexate is a competitive inhibitor that can bind to and inhibit the <scene name='42/420816/Cv/6'>~~TextToBeDisplayed~~</scene>. The active site is buried within the enzyme as is depicted by the <scene name='Sandbox_58/Solvent_accessable_surface/1'>solvent accessable surface</scene> shown in orange at the entrance to the active site. The

The nature of this binding has a 1000 fold increase in affinity relative to the natural folate affinity of DHFR, producing a practically irreversible inhibition of DHFR activity. Methotrexate is a competitive inhibitor that can bind to and inhibit the <scene name='42/420816/Cv/6'>active site of human DHFR</scene> ([[1u72]]). The active site is buried within the enzyme as is depicted by the <scene name='Sandbox_58/Solvent_accessable_surface/1'>solvent accessable surface</scene> shown in orange at the entrance to the active site. The

<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.

[[Image:2011-03-10_0224.png|400px|left|thumb| Methotrexate Residue Interaction <ref>DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE. (n.d.). RCSB Protein Database. Retrieved March 10, 2011, from www.rcsb.org/pdb/results </ref>]]

[[Image:DHFR ligands.png|400px|left|thumb| DHFR substrates <ref>Enzymes. (n.d.). Oregon State University. Retrieved March 10, 2011, from http://oregonstate.edu/instruction/bb450/fall2010/lecture/enzymesoutline.html </ref>]]

Methotrexate: Difference between revisions

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-The nature of this binding has a 1000 fold increase in affinity relative to the natural folate affinity of DHFR , producing a practically irreversible inhibition of DHFR activity.  Methotrexate is a competitive inhibitor that can bind to and inhibit the <scene name='42/420816/Cv/6'>TextToBeDisplayed</scene>. The active site is buried within the enzyme as is depicted by the <scene name='Sandbox_58/Solvent_accessable_surface/1'>solvent accessable surface</scene> shown in orange at the entrance to the active site.  The
+The nature of this binding has a 1000 fold increase in affinity relative to the natural folate affinity of DHFR, producing a practically irreversible inhibition of DHFR activity.  Methotrexate is a competitive inhibitor that can bind to and inhibit the <scene name='42/420816/Cv/6'>active site of human DHFR</scene> ([[1u72]]). The active site is buried within the enzyme as is depicted by the <scene name='Sandbox_58/Solvent_accessable_surface/1'>solvent accessable surface</scene> shown in orange at the entrance to the active site.  The
 <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.
-[[Image:2011-03-10_0224.png|400px|left|thumb| Methotrexate Residue Interaction <ref>DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE. (n.d.). RCSB Protein Database. Retrieved March 10, 2011, from www.rcsb.org/pdb/results </ref>]]
 [[Image:DHFR ligands.png|400px|left|thumb| DHFR substrates <ref>Enzymes. (n.d.). Oregon State University. Retrieved March 10, 2011, from http://oregonstate.edu/instruction/bb450/fall2010/lecture/enzymesoutline.html </ref>]]