More MS news articles for May 2002

Crystal structure and biochemical characterization of human kallikrein 6 reveals a trypsin-like kallikrein is expressed in the central nervous system

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11983703&dopt=Abstract

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http://www.jbc.org/cgi/reprint/M202392200v1.pdf

J Biol Chem 2002 Apr 30
Bernett MJ, Blaber SI, Scarisbrick IA, Dhanarajan P, Thompson SM, Blaber M.
Chemistry and Biochemistry, Florida State University, Tallahassee, Fl 32306-4380.

The human kallikreins are a large multi-gene family of closely-related serine-type proteases.

In this regard, they are similar to the multi-gene kallikrein families characterized in the mouse and rat.

There is a much more extensive body of knowledge regarding the function of mouse and rat kallikreins in comparison to 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 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 is presented that supports the identification of human kallikrein 6 as the functional homologue of rat myelencephalon specific protease and is corroborated by a molecular phylogenetic analysis.

Furthermore, the x-ray data provides support for the characterization of human kallikrein 6 as a degradative protease with structural features more similar to trypsin than the regulatory kallikreins.