1ao5: Difference between revisions
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 15:45, 30 October 2007
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MOUSE GLANDULAR KALLIKREIN-13 (PRORENIN CONVERTING ENZYME)
OverviewOverview
A crystal structure of the serine protease, mouse glandular kallikrein 13, (mGK-13) has been determined at 2.6-A resolution. This enzyme, isolated, from the mouse submandibular gland, is also known as prorenin-converting, enzyme and cleaves submandibular gland Ren-2 prorenin to yield active, renin. The mGK-13 structure is similar to other members of the mammalian, serine protease family, having five conserved disulfide bonds and an, active site located in the cleft between two beta-barrel domains. The, mGK-13 structure reveals for the first time an ordered kallikrein loop, conformation containing a short 3(10) helix. This loop is disordered in, the related porcine pancreatic kallikrein and rat submandibular tonin, structures. The kallikrein loop is in close spatial proximity to the, ... [(full description)]
About this StructureAbout this Structure
1AO5 is a [Single protein] structure of sequence from [Mus musculus]. Active as [Tissue kallikrein], with EC number [3.4.21.35]. Structure known Active Sites: A and B. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme)., Timm DE, Protein Sci. 1997 Jul;6(7):1418-25. PMID:9232643
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