1hpt
From Proteopedia
(Difference between revisions)
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<StructureSection load='1hpt' size='340' side='right'caption='[[1hpt]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1hpt' size='340' side='right'caption='[[1hpt]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1hpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1hpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HPT FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpt OCA], [https://pdbe.org/1hpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hpt RCSB], [https://www.ebi.ac.uk/pdbsum/1hpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hpt ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpt OCA], [https://pdbe.org/1hpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hpt RCSB], [https://www.ebi.ac.uk/pdbsum/1hpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hpt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/ISK1_HUMAN ISK1_HUMAN] Defects in SPINK1 are a cause of pancreatitis (PCTT) [MIM:[https://omim.org/entry/167800 167800]. A disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks.<ref>PMID:10835640</ref> <ref>PMID:10691414</ref> <ref>PMID:12974284</ref> Defects in SPINK1 are the cause of susceptibility to tropical calcific pancreatitis (TCP) [MIM:[https://omim.org/entry/608189 608189]. TCP is an idiopathic, juvenile, nonalcoholic form of chronic pancreatitis widely prevalent in several tropical countries. It can be associated with fibrocalculous pancreatic diabetes (FCPD) depending on both environmental and genetic factors. TCP differs from alcoholic pancreatitis by a much younger age of onset, pancreatic calcification, a high incidence of insulin dependent but ketosis resistant diabetes mellitus, and an exceptionally high incidence of pancreatic cancer.<ref>PMID:12187509</ref> <ref>PMID:12011155</ref> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ISK1_HUMAN ISK1_HUMAN] This is a trypsin inhibitor, its physiological function is to prevent the trypsin-catalyzed premature activation of zymogens within the pancreas. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hpt ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hpt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | A modified version of the human pancreatic trypsin inhibitor (PSTI), generated in a protein-design project, has been crystallized in spacegroup P4(3) with lattice constants a = 40.15 A, c = 33.91 A. The structure has been solved by molecular replacement. Refinement of the structure by simulated annealing and conventional restrained least-squares yielded for 8.0 to 2.3 A data a final R-value of 19.1%. Differences to the known structures of porcine PSTI complexed with trypsinogen and modified human PSTI complexed with chymotrypsinogen occur at the flexible N-terminal part of the molecule. These differences are influenced by crystal packing, as are low temperature factors for the binding loop. The geometry of the binding loop is similar to the complexed structures. | ||
- | |||
- | Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type).,Hecht HJ, Szardenings M, Collins J, Schomburg D J Mol Biol. 1992 Jun 20;225(4):1095-103. PMID:1613792<ref>PMID:1613792</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1hpt" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Collins | + | [[Category: Collins J]] |
- | [[Category: Hecht | + | [[Category: Hecht HJ]] |
- | [[Category: Schomburg | + | [[Category: Schomburg D]] |
- | [[Category: Szardenings | + | [[Category: Szardenings M]] |
- | + |
Revision as of 11:34, 27 March 2024
THREE-DIMENSIONAL STRUCTURE OF A RECOMBINANT VARIANT OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL TYPE)
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