1eou

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==Overview==
==Overview==
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The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the, widely used anti-epileptic drug topiramate, possesses anti-convulsant and, carbonic anhydrase-inhibitory activities. We have studied the binding, interactions of RWJ-37497 in the active site of human carbonic anhydrase, II by X-ray crystallography. The atomic positions of the enzyme inhibitor, complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final, crystallographic R and R(free) values of 0.18 and 0.23, respectively. The, inhibitor co-ordinates to the active-site zinc ion through its oxygen atom, and the ionized nitrogen atom of the sulphamate group by replacing the, metal-bound water molecules, although the sulphamoyl oxygen atom provides, a rather lengthy co-ordination. The 4,5-cyclic sulphate group is, positioned in a hydrophobic pocket of the active site, making contacts, with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand, was found to be intact, concerns about RWJ-37947 irreversibly alkylating, the enzyme through its 4,5-cyclic sulphate group were dispelled.
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The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled.
==Disease==
==Disease==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chattopadhyay, D.]]
[[Category: Chattopadhyay, D.]]
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[[Category: Costanzo, M.J.]]
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[[Category: Costanzo, M J.]]
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[[Category: Maryanoff, B.E.]]
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[[Category: Maryanoff, B E.]]
[[Category: Recacha, R.]]
[[Category: Recacha, R.]]
[[Category: SMS]]
[[Category: SMS]]
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[[Category: protein-inhibitor complex]]
[[Category: protein-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:44:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:00 2008''

Revision as of 10:30, 21 February 2008


1eou, resolution 2.10Å

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CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE

Contents

Overview

The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

1EOU is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate., Recacha R, Costanzo MJ, Maryanoff BE, Chattopadhyay D, Biochem J. 2002 Feb 1;361(Pt 3):437-41. PMID:11802772

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