2q1q
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Sulthiame, a clinically used antiepileptic, was investigated for its | + | Sulthiame, a clinically used antiepileptic, was investigated for its interaction with 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms. The drug is a potent inhibitor of CA II, VII, IX, and XII (K(I)s of 6-56 nM), and a medium potency inhibitor against CA IV, VA, VB, and VI (K(I)s of 81-134 nM). The high resolution crystal structure of the hCA II-sulthiame adduct revealed a large number of favorable interactions between the drug and the enzyme which explain its strong low nanomolar affinity for this isoform and may also be exploited for the design of effective inhibitors incorporating sultam moieties. |
| + | |||
| + | ==Disease== | ||
| + | Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611492 611492]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 13: | ||
==Reference== | ==Reference== | ||
| - | Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: | + | Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies., Temperini C, Innocenti A, Mastrolorenzo A, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2007 Sep 1;17(17):4866-72. Epub 2007 Jun 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17588751 17588751] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 16: | Line 19: | ||
[[Category: Mastrolorenzo, A.]] | [[Category: Mastrolorenzo, A.]] | ||
[[Category: Scozzafava, A.]] | [[Category: Scozzafava, A.]] | ||
| - | [[Category: Supuran, C | + | [[Category: Supuran, C T.]] |
[[Category: Temperini, C.]] | [[Category: Temperini, C.]] | ||
[[Category: HG]] | [[Category: HG]] | ||
| Line 27: | Line 30: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:07 2008'' |
Revision as of 16:35, 21 February 2008
|
Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-Ray crystallographic studies
Contents |
Overview
Sulthiame, a clinically used antiepileptic, was investigated for its interaction with 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms. The drug is a potent inhibitor of CA II, VII, IX, and XII (K(I)s of 6-56 nM), and a medium potency inhibitor against CA IV, VA, VB, and VI (K(I)s of 81-134 nM). The high resolution crystal structure of the hCA II-sulthiame adduct revealed a large number of favorable interactions between the drug and the enzyme which explain its strong low nanomolar affinity for this isoform and may also be exploited for the design of effective inhibitors incorporating sultam moieties.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
2Q1Q is a Single protein structure of sequence from [1] with , and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies., Temperini C, Innocenti A, Mastrolorenzo A, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2007 Sep 1;17(17):4866-72. Epub 2007 Jun 14. PMID:17588751
Page seeded by OCA on Thu Feb 21 18:35:07 2008
