1aef: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1AEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 3AP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | 1AEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 3AP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEF OCA]]. | ||
==Reference== | ==Reference== | ||
Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein., Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, J Mol Biol. 2002 Jan 25;315(4):845-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11812152 11812152] | Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein., Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, J Mol Biol. 2002 Jan 25;315(4):845-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11812152 11812152] | ||
[[Category: Cytochrome-c peroxidase]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:39:01 2007'' | ||
Revision as of 11:34, 30 October 2007
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SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (3-AMINOPYRIDINE)
OverviewOverview
Cavity complementation has been observed in many proteins, where an, appropriate small molecule binds to a cavity-forming mutant. Here, the, binding of compounds to the W191G cavity mutant of cytochrome c peroxidase, is characterized by X-ray crystallography and binding thermodynamics., Unlike cavities created by removal of hydrophobic side-chains, the W191G, cavity does not bind neutral or hydrophobic compounds, but displays a, strong specificity for heterocyclic cations, consistent with the role of, the protein to stabilize a tryptophan radical at this site. Ligand, dissociation constants for the protonated cationic state ranged from 6, microM for 2-amino-5-methylthiazole to 1 mM for neutral ligands, and, binding was associated with a large enthalpy-entropy compensation. X-ray, ... [(full description)]
About this StructureAbout this Structure
1AEF is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and 3AP as [ligands]. Active as [Cytochrome-c peroxidase], with EC number [1.11.1.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
ReferenceReference
Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein., Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, J Mol Biol. 2002 Jan 25;315(4):845-57. PMID:11812152
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