2qn5: Difference between revisions
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c2a|1c2a]], [[1tx6|1tx6]], [[1k9b|1k9b]], [[1s0q|1s0q]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c2a|1c2a]], [[1tx6|1tx6]], [[1k9b|1k9b]], [[1s0q|1s0q]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2qn5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn5 OCA], [http://pdbe.org/2qn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2qn5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2qn5" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin|Trypsin]] | ||
*[[Trypsin inhibitor|Trypsin inhibitor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:06, 10 September 2015
Crystal Structure and Functional Study of the Bowman-Birk Inhibitor from Rice Bran in Complex with Bovine TrypsinCrystal Structure and Functional Study of the Bowman-Birk Inhibitor from Rice Bran in Complex with Bovine Trypsin
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 A. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%. Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa.,Lin YH, Li HT, Huang YC, Hsieh YC, Guan HH, Liu MY, Chang T, Wang AH, Chen CJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):522-4. Epub 2006 May 5. PMID:16754971[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bos taurus
- Oryza sativa
- Trypsin
- Chen, C J
- Guan, H H
- Hsieh, Y C
- Li, H T
- Lin, Y H
- Wang, A H.J
- Bowman-birk inhibitor
- Digestion
- Hetero-dimer
- Hydrolase
- Hydrolase inhibitor-hydrolase complex
- Metal-binding
- Monocotyledonous plant
- Plant-pest system
- Protease inhibitor
- Protease-inhibitor
- Rbti
- Reactive-site loop
- Secreted
- Serine protease inhibitor
- Zymogen