1dhf

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[[Image:1dhf.gif|left|200px]]
[[Image:1dhf.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dhf |SIZE=350|CAPTION= <scene name='initialview01'>1dhf</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1dhf", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1dhf| PDB=1dhf | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhf OCA], [http://www.ebi.ac.uk/pdbsum/1dhf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dhf RCSB]</span>
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}}
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'''CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE'''
'''CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE'''
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[[Category: /II, J F.Davies.]]
[[Category: /II, J F.Davies.]]
[[Category: Kraut, J.]]
[[Category: Kraut, J.]]
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[[Category: oxido-reductase]]
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[[Category: Oxido-reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:36 2008''
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Revision as of 10:51, 2 May 2008

Image:1dhf.gif

Template:STRUCTURE 1dhf

CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE


Overview

The 2.3-A crystal structure of recombinant human dihydrofolate reductase (EC 1.5.1.3, DHFR) has been solved as a binary complex with folate (a poor substrate at neutral pH) and also as a binary complex with an inhibitor, 5-deazafolate. The inhibitor appears to be protonated at N8 on binding, whereas folate is not. Rotation of the peptide plane joining I7 and V8 from its position in the folate complex permits hydrogen bonding of 5-deazafolate's protonated N8 to the backbone carbonyl of I7, thus contributing to the enzyme's greater affinity for 5-deazafolate than for folate. In this respect it is likely that bound 5-deazafolate furnishes a model for 7,8-dihydrofolate binding and, in addition, resembles the transition state for folate reduction. A hypothetical transition-state model for folate reduction, generated by superposition of the DHFR binary complexes human.5-deazafolate and chicken liver.NADPH, reveals a 1-A overlap of the binding sites for folate's pteridine ring and the dihydronicotinamide ring of NADPH. It is proposed that this binding-site overlap accelerates the reduction of both folate and 7,8-dihydrofolate by simultaneously binding substrate and cofactor with a sub van der Waals separation that is optimal for hydride transfer.

About this Structure

1DHF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate., Davies JF 2nd, Delcamp TJ, Prendergast NJ, Ashford VA, Freisheim JH, Kraut J, Biochemistry. 1990 Oct 9;29(40):9467-79. PMID:2248959 Page seeded by OCA on Fri May 2 13:51:02 2008

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