1dhr: Difference between revisions

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[[Image:1dhr.~~gif~~|left|200px]]

[[Image:1dhr.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE~~'''~~

===CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE===

~~==Overview==~~

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The ~~structure of a binary complex of dihydropteridine reductase [DHPR; NAD~~(~~P)H~~:~~6,7-dihydropteridine oxidoreductase, EC 1~~.6.~~99.7] with its cofactor~~, ~~NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR~~ is ~~an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in~~ the ~~human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface~~. ~~Dimerization is mediated by a four~~-~~helix bundle motif (two helices from each protomer) having an unusual right~~-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase.

The line below this paragraph, {{ABSTRACT_PUBMED_1631094}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 1631094 is the PubMed ID number.

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==About this Structure==

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[[Category: Whiteley, J M.]]

[[Category: Xuong, N H.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:51:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:04:54 2008''

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-[[Image:1dhr.gif|left|200px]]
+{{Seed}}
+[[Image:1dhr.png|left|200px]]
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 {{STRUCTURE_1dhr|  PDB=1dhr  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE'''
+===CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE===
-==Overview==
+<!--
-The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase.
+The line below this paragraph, {{ABSTRACT_PUBMED_1631094}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1631094 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1631094}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Whiteley, J M.]]
 [[Category: Xuong, N H.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:51:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:04:54 2008''