2ra3

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[[Image:2ra3.png|left|200px]]
 
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{{STRUCTURE_2ra3| PDB=2ra3 | SCENE= }}
{{STRUCTURE_2ra3| PDB=2ra3 | SCENE= }}
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===Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI)===
===Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI)===
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{{ABSTRACT_PUBMED_18077447}}
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{{ABSTRACT_PUBMED_18077447}}
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==Disease==
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[[http://www.uniprot.org/uniprot/TRY1_HUMAN TRY1_HUMAN]] Defects in PRSS1 are a cause of pancreatitis (PCTT) [MIM:[http://omim.org/entry/167800 167800]]. A disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks.<ref>PMID:10930381</ref><ref>PMID:8841182</ref><ref>PMID:11866271</ref><ref>PMID:9322498</ref><ref>PMID:9633818</ref><ref>PMID:10381903</ref><ref>PMID:10204851</ref><ref>PMID:11073545</ref><ref>PMID:11788572</ref><ref>PMID:14695529</ref><ref>PMID:15776435</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/TRY1_HUMAN TRY1_HUMAN]] Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.<ref>PMID:7945238</ref> [[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:018077447</ref><references group="xtra"/>
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<ref group="xtra">PMID:018077447</ref><references group="xtra"/><references/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 04:26, 25 March 2013

Template:STRUCTURE 2ra3

Contents

Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI)

Template:ABSTRACT PUBMED 18077447

Disease

[TRY1_HUMAN] Defects in PRSS1 are a cause of pancreatitis (PCTT) [MIM:167800]. A disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks.[1][2][3][4][5][6][7][8][9][10][11]

Function

[TRY1_HUMAN] Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.[12] [BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.

About this Structure

2ra3 is a 4 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Salameh MA, Soares AS, Hockla A, Radisky ES. Structural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsin. J Biol Chem. 2008 Feb 15;283(7):4115-23. Epub 2007 Dec 12. PMID:18077447 doi:10.1074/jbc.M708268200
  1. ↑ Teich N, Ockenga J, Hoffmeister A, Manns M, Mossner J, Keim V. Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation. Gastroenterology. 2000 Aug;119(2):461-5. PMID:10930381
  2. ↑ Whitcomb DC, Gorry MC, Preston RA, Furey W, Sossenheimer MJ, Ulrich CD, Martin SP, Gates LK Jr, Amann ST, Toskes PP, Liddle R, McGrath K, Uomo G, Post JC, Ehrlich GD. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nat Genet. 1996 Oct;14(2):141-5. PMID:8841182 doi:10.1038/ng1096-141
  3. ↑ Teich N, Bauer N, Mossner J, Keim V. Mutational screening of patients with nonalcoholic chronic pancreatitis: identification of further trypsinogen variants. Am J Gastroenterol. 2002 Feb;97(2):341-6. PMID:11866271 doi:10.1111/j.1572-0241.2002.05467.x
  4. ↑ Gorry MC, Gabbaizedeh D, Furey W, Gates LK Jr, Preston RA, Aston CE, Zhang Y, Ulrich C, Ehrlich GD, Whitcomb DC. Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. Gastroenterology. 1997 Oct;113(4):1063-8. PMID:9322498
  5. ↑ Teich N, Mossner J, Keim V. Mutations of the cationic trypsinogen in hereditary pancreatitis. Hum Mutat. 1998;12(1):39-43. PMID:9633818 doi:<39::AID-HUMU6>3.0.CO;2-P 10.1002/(SICI)1098-1004(1998)12:1<39::AID-HUMU6>3.0.CO;2-P
  6. ↑ Witt H, Luck W, Becker M. A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis. Gastroenterology. 1999 Jul;117(1):7-10. PMID:10381903
  7. ↑ Ferec C, Raguenes O, Salomon R, Roche C, Bernard JP, Guillot M, Quere I, Faure C, Mercier B, Audrezet MP, Guillausseau PJ, Dupont C, Munnich A, Bignon JD, Le Bodic L. Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis. J Med Genet. 1999 Mar;36(3):228-32. PMID:10204851
  8. ↑ Chen JM, Raguenes O, Ferec C, Deprez PH, Verellen-Dumoulin C. A CGC>CAT gene conversion-like event resulting in the R122H mutation in the cationic trypsinogen gene and its implication in the genotyping of pancreatitis. J Med Genet. 2000 Nov;37(11):E36. PMID:11073545
  9. ↑ Pfutzer R, Myers E, Applebaum-Shapiro S, Finch R, Ellis I, Neoptolemos J, Kant JA, Whitcomb DC. Novel cationic trypsinogen (PRSS1) N29T and R122C mutations cause autosomal dominant hereditary pancreatitis. Gut. 2002 Feb;50(2):271-2. PMID:11788572
  10. ↑ Teich N, Le Marechal C, Kukor Z, Caca K, Witzigmann H, Chen JM, Toth M, Mossner J, Keim V, Ferec C, Sahin-Toth M. Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2). Hum Mutat. 2004 Jan;23(1):22-31. PMID:14695529 doi:10.1002/humu.10285
  11. ↑ Teich N, Nemoda Z, Kohler H, Heinritz W, Mossner J, Keim V, Sahin-Toth M. Gene conversion between functional trypsinogen genes PRSS1 and PRSS2 associated with chronic pancreatitis in a six-year-old girl. Hum Mutat. 2005 Apr;25(4):343-7. PMID:15776435 doi:10.1002/humu.20148
  12. ↑ Koshikawa N, Yasumitsu H, Nagashima Y, Umeda M, Miyazaki K. Identification of one- and two-chain forms of trypsinogen 1 produced by a human gastric adenocarcinoma cell line. Biochem J. 1994 Oct 1;303 ( Pt 1):187-90. PMID:7945238

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