1cnw
From Proteopedia
(New page: 200px<br /> <applet load="1cnw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cnw, resolution 2.0Å" /> '''SECONDARY INTERACTIO...) |
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caption="1cnw, resolution 2.0Å" /> | caption="1cnw, resolution 2.0Å" /> | ||
'''SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS'''<br /> | '''SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CNW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, HG and EG1 as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CNW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb49_1.html Carbonic Anhydrase]]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http:// | + | 1CNW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=EG1:'>EG1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CNW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb49_1.html Carbonic Anhydrase]]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lyase (oxo-acid)]] | [[Category: lyase (oxo-acid)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:36:25 2008'' |
Revision as of 13:36, 15 February 2008
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SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
Contents |
Overview
A series of competitive inhibitors of carbonic anhydrase II (CAII; EC, 4.2.1.1) that consists of oligo(ethylene glycol) units attached to, p-benzenesulfonamides with pendant amino acids, H2NSO2C6H4CONHCH2CH2OCH2CH2OCH2CH2NHCOCHRNH3+, have been synthesized and, examined using competitive fluorescence assays. Three of the strongest, inhibitors, designated EG3NH3+, EG3GlyNH3+, and EG3PheNH3+, have been, studied by X-ray crystallographic methods at limiting resolutions of 1.9, 2.0, and 2.3 A, respectively. The sulfonamide-zinc binding modes and the, association of the ethylene glycol linkers to the hydrophobic patch of the, active site are similar in all three inhibitors. Differences in the values, of Kd are therefore not due to differences in zinc coordination or to, differences in the modes of enzyme-glycol association but instead appear, to arise from interaction of the pendant amino acids with the surface of, the protein. These pendant groups are, however, not sufficiently ordered, to be visible in electron density maps. Thus, structural variations of, inhibitors at locations distant from the primary binding (i.e., the, sulfonamide group) site affect the overall binding affinities of, inhibitors (e.g., Kd (EG3PheNH3+) = 14 nM as compared with Kd (EG3GluNH3+), = 100 nM).
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1CNW is a Single protein structure of sequence from Homo sapiens with , and as ligands. The following page contains interesting information on the relation of 1CNW with [Carbonic Anhydrase]. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants., Boriack PA, Christianson DW, Kingery-Wood J, Whitesides GM, J Med Chem. 1995 Jun 23;38(13):2286-91. PMID:7608893
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