1vgc: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1VGC is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with SO4 and V36 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | 1VGC is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with SO4 and V36 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VGC OCA]]. | ||
==Reference== | ==Reference== | ||
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9425066 9425066] | Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9425066 9425066] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chymotrypsin]] | |||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Eger, B.T.]] | [[Category: Eger, B.T.]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''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 10:39:34 2007'' | ||
Revision as of 11:34, 30 October 2007
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GAMMA-CHYMOTRYPSIN L-PARA-CHLORO-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
OverviewOverview
In order to probe the structural basis of stereoselectivity in the serine, protease family, a series of enantiomeric boronic acids, RCH2CH(NHCOCH3)B(OH)2 has been synthesized and kinetically characterized, as transition-state analog inhibitors using alpha-chymotrypsin and, subtilisin Carlsberg as model systems. When the R-substituent in this, series was changed from a p-chlorophenyl to a 1-naphthyl group, alpha-chymotrypsin, but not subtilisin, reversed its usual preference for, l-enantiomers and bound more tightly to the D-enantiomer [Martichonok, V., & Jones, J. B. (1996) J. Am. Chem. Soc. 118, 950-958]. The structural, factors responsible for the differences in stereoselectivity between the, two enzymes have been explored by X-ray crystallographic examination of, subtilisin ... [(full description)]
About this StructureAbout this Structure
1VGC is a [Protein complex] structure of sequences from [Bos taurus] with SO4 and V36 as [ligands]. Active as [Chymotrypsin], with EC number [3.4.21.1]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:9425066
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