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1pi2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pi2' size='340' side='right'caption='[[1pi2]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1pi2' size='340' side='right'caption='[[1pi2]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1pi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PI2 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=1pi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi2 OCA], [https://pdbe.org/1pi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi2 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]] 2.5Å</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=1pi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi2 OCA], [https://pdbe.org/1pi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IBBD2_SOYBN IBBD2_SOYBN] | ||
== 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=1pi2 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=1pi2 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-II) has been determined by x-ray crystallography and refined at 2.5-A resolution. This protein is a specific inhibitor of trypsin. Two reactive site loops, one at each end of the PI-II molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr. B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure to be refined at high resolution, providing further insight into inhibitor mechanisms. | ||
| - | |||
| - | Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.,Chen P, Rose J, Love R, Wei CH, Wang BC J Biol Chem. 1992 Jan 25;267(3):1990-4. PMID:1730730<ref>PMID:1730730</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pi2" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Glycine | + | [[Category: Glycine max]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chen | + | [[Category: Chen P]] |
| - | [[Category: Rose | + | [[Category: Rose J]] |
| - | [[Category: Wang | + | [[Category: Wang BC]] |
| - | + | ||
Current revision
REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS
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Categories: Glycine max | Large Structures | Chen P | Rose J | Wang BC
