1l2e
From Proteopedia
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|PDB= 1l2e |SIZE=350|CAPTION= <scene name='initialview01'>1l2e</scene>, resolution 1.75Å | |PDB= 1l2e |SIZE=350|CAPTION= <scene name='initialview01'>1l2e</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2e OCA], [http://www.ebi.ac.uk/pdbsum/1l2e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l2e RCSB]</span> | ||
}} | }} | ||
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[[Category: Blaber, S I.]] | [[Category: Blaber, S I.]] | ||
[[Category: Scarisbrick, I A.]] | [[Category: Scarisbrick, I A.]] | ||
| - | [[Category: BEN]] | ||
| - | [[Category: MG]] | ||
[[Category: benzamidine]] | [[Category: benzamidine]] | ||
[[Category: human kallikrein 6]] | [[Category: human kallikrein 6]] | ||
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[[Category: zyme]] | [[Category: zyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:57:04 2008'' |
Revision as of 18:57, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Human Kallikrein 6 (hK6) Active Form with benzamidine inhibitor
Overview
The human kallikreins are a large multigene family of closely related serine-type proteases. In this regard, they are similar to the multigene kallikrein families characterized in mice and rats. There is a much more extensive body of knowledge regarding the function of mouse and rat kallikreins in comparison with the human kallikreins. Human kallikrein 6 has been proposed as the homologue to rat myelencephalon-specific protease, an arginine-specific degradative-type protease abundantly expressed in the central nervous system and implicated in demyelinating disease. We present the x-ray crystal structure of mature, active recombinant human kallikrein 6 at 1.75-A resolution. This high resolution model provides the first three-dimensional view of one of the human kallikreins and one of only a few structures of serine proteases predominantly expressed in the central nervous system. Enzymatic data are presented that support the identification of human kallikrein 6 as the functional homologue of rat myelencephalon-specific protease and are corroborated by a molecular phylogenetic analysis. Furthermore, the x-ray data provide support for the characterization of human kallikrein 6 as a degradative protease with structural features more similar to trypsin than the regulatory kallikreins.
About this Structure
1L2E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system., Bernett MJ, Blaber SI, Scarisbrick IA, Dhanarajan P, Thompson SM, Blaber M, J Biol Chem. 2002 Jul 5;277(27):24562-70. Epub 2002 Apr 30. PMID:11983703
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