1cjl: Difference between revisions
New page: left|200px<br /> <applet load="1cjl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjl, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF... |
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==About this Structure== | ==About this Structure== | ||
1CJL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJL OCA]]. | 1CJL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJL OCA]]. | ||
==Reference== | ==Reference== | ||
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment., Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort JS, Cygler M, EMBO J. 1996 Oct 15;15(20):5492-503. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8896443 8896443] | Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment., Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort JS, Cygler M, EMBO J. 1996 Oct 15;15(20):5492-503. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8896443 8896443] | ||
[[Category: Cathepsin L]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: propeptide]] | [[Category: propeptide]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:44:49 2007'' | ||
Revision as of 14:40, 30 October 2007
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CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM
OverviewOverview
Cathepsin L is a member of the papain superfamily of cysteine proteases, and, like many other proteases, it is synthesized as an inactive, proenzyme. Its prosegment shows little homology to that of procathepsin B, whose structure, the first for a cysteine protease proenzyme, has been, determined recently. We report here the 3-D structure of a mutant of human, procathepsin L determined at 2.2 A resolution, describe the mode of, binding employed by the prosegment and discuss the molecular basis for, other possible roles of the prosegment. The N-terminal part of the, prosegment is globular and contains three alpha-helices with a small, hydrophobic core built around aromatic side chains. This domain packs, against a loop on the enzyme's surface, with the aromatic side chain from, the ... [(full description)]
About this StructureAbout this Structure
1CJL is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Cathepsin L], with EC number [3.4.22.15]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment., Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort JS, Cygler M, EMBO J. 1996 Oct 15;15(20):5492-503. PMID:8896443
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