2fzh: Difference between revisions

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{{Seed}}
[[Image:2fzh.png|left|200px]]
[[Image:2fzh.png|left|200px]]


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==About this Structure==
==About this Structure==
2FZH is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Pneumocystis_carinii Pneumocystis carinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZH OCA].  
[[2fzh]] is a 1 chain structure of [[Dihydrofolate reductase]] with sequence from [http://en.wikipedia.org/wiki/Pneumocystis_carinii Pneumocystis carinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZH OCA].  
 
==See Also==
*[[Dihydrofolate reductase]]


==Reference==
==Reference==
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[[Category: Rosowsky, A.]]
[[Category: Rosowsky, A.]]
[[Category: Dihydrofolate reductase]]
[[Category: Dihydrofolate reductase]]
[[Category: Oxidoreductase]]
[[Category: Ring stacking interaction]]
[[Category: Ring stacking interaction]]
[[Category: Trimethoprim derivative]]
[[Category: Trimethoprim derivative]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:56:33 2009''

Revision as of 04:22, 27 December 2010

File:2fzh.png

Template:STRUCTURE 2fzh

New Insights into Dihydrofolate Reductase Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim DerivativesNew Insights into Dihydrofolate Reductase Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim Derivatives

Template:ABSTRACT PUBMED 17019704

About this StructureAbout this Structure

2fzh is a 1 chain structure of Dihydrofolate reductase with sequence from Pneumocystis carinii. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Cody V, Pace J, Chisum K, Rosowsky A. New insights into DHFR interactions: analysis of Pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent 5-(omega-carboxy(alkyloxy) trimethoprim derivatives reveals conformational correlations with activity and novel parallel ring stacking interactions. Proteins. 2006 Dec 1;65(4):959-69. PMID:17019704 doi:10.1002/prot.21131

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