1l2e

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bernett, M.J.]]
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[[Category: Bernett, M J.]]
[[Category: Blaber, M.]]
[[Category: Blaber, M.]]
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[[Category: Blaber, S.I.]]
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[[Category: Blaber, S I.]]
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[[Category: Scarisbrick, I.A.]]
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[[Category: Scarisbrick, I A.]]
[[Category: BEN]]
[[Category: BEN]]
[[Category: MG]]
[[Category: MG]]
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[[Category: zyme]]
[[Category: zyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:16:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:31 2008''

Revision as of 11:40, 21 February 2008


1l2e, resolution 1.75Å

Drag the structure with the mouse to rotate

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 with and as ligands. 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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