1ao5: Difference between revisions
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==Overview== | ==Overview== | ||
A crystal structure of the serine protease, mouse glandular kallikrein 13 | 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 active site and is also involved in a dimeric arrangement of mGK-13. The catalytic specificity of mGK-13 for Ren-2 prorenin was studied by modeling a prorenin-derived peptide into the active site of mGK-13. This model emphasizes two electronegative substrate specificity pockets on the mGK-13 surface, which could accommodate the dibasic P2 and P1 residues at the site of prorenin cleavage by mGK-13. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tissue kallikrein]] | [[Category: Tissue kallikrein]] | ||
[[Category: Timm, D | [[Category: Timm, D E.]] | ||
[[Category: glandular kallikrein]] | [[Category: glandular kallikrein]] | ||
[[Category: protein maturation]] | [[Category: protein maturation]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:34 2008'' | ||
Revision as of 12:46, 21 February 2008
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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 active site and is also involved in a dimeric arrangement of mGK-13. The catalytic specificity of mGK-13 for Ren-2 prorenin was studied by modeling a prorenin-derived peptide into the active site of mGK-13. This model emphasizes two electronegative substrate specificity pockets on the mGK-13 surface, which could accommodate the dibasic P2 and P1 residues at the site of prorenin cleavage by mGK-13.
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 Known structural/functional Sites: and . 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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