2fmg: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2FMG is a | 2FMG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMG OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:16686544</ref><references group="xtra"/> | |||
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Scozzafava, A.]] | [[Category: Scozzafava, A.]] | ||
[[Category: Supuran, C T.]] | [[Category: Supuran, C T.]] | ||
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[[Category: Carbonic anhydrase ii]] | [[Category: Carbonic anhydrase ii]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:32:18 2009'' |
Revision as of 07:32, 17 February 2009
Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine and crystallographic analysis of their adducts with isozyme II: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanineCarbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine and crystallographic analysis of their adducts with isozyme II: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanine
Template:ABSTRACT PUBMED 16686544
About this StructureAbout this Structure
2FMG is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Temperini C, Scozzafava A, Vullo D, Supuran CT. Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design. J Med Chem. 2006 May 18;49(10):3019-27. PMID:16686544 doi:10.1021/jm0603320
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