Sandbox Reserved 1091: Difference between revisions
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'''The P-domain:''' The core of the P-domain in ASP contains 8 béta-strands (béta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/2'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/3'>pL1</scene>(Gly 521–Thr 525, béta 5, 6, and 12) and <scene name='82/829344/Pl2/3'>pL2</scene> (Gly-557–Asn-578, béta 25), and it is situated close to <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> Asp-78,His-115,and Ser-336. | '''The P-domain:''' The core of the P-domain in ASP contains 8 béta-strands (béta 16 18 23 and 26). The <scene name='82/829344/Extra_occluding_region/2'>extra occluding-region</scene> is comprised of two parts, <scene name='82/829344/Pl1/3'>pL1</scene>(Gly 521–Thr 525, béta 5, 6, and 12) and <scene name='82/829344/Pl2/3'>pL2</scene> (Gly-557–Asn-578, béta 25), and it is situated close to <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> Asp-78,His-115,and Ser-336. | ||
All these domains are represented schematically in the article <ref>Structural Basis for the Kexin-like Serine Protease from Aeromonas sobria as Sepsis-causing Factor. H Kobayashi et al. J Biol Chem. 284(40): 27655–27663 (2009)</ref> : [ | All these domains are represented schematically in the article <ref>Structural Basis for the Kexin-like Serine Protease from Aeromonas sobria as Sepsis-causing Factor. H Kobayashi et al. J Biol Chem. 284(40): 27655–27663 (2009)</ref> : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F2/ '''representation 2D of ASP'''] | ||
On these figures, we can see the different domains of the protein in A and also a superposition with the Kex2. We clearly see the resemblance between both serine protease, and the extra occluding region in the C-terminal region of ASP. | |||
