1bi6
From Proteopedia
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- | [[Image:1bi6.png|left|200px]] | ||
- | + | ==NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM== | |
+ | <StructureSection load='1bi6' size='340' side='right'caption='[[1bi6]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1bi6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ananas_comosus Ananas comosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BI6 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1bi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi6 OCA], [https://pdbe.org/1bi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bi6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bi6 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/IBRO_ANACO IBRO_ANACO] Weak inhibitor of cysteine proteinases. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bromelain inhibitor VI from pineapple stem (BI-VI) is a unique double-chain inhibitor with an 11-residue light chain and a 41-residue heavy chain by disulfide bonds and inhibits the cysteine proteinase bromelain competitively. The structure of BI-VI in aqueous solution was determined using nuclear magnetic resonance spectroscopy and simulated annealing-based calculations. Its three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded antiparallel beta-sheet. Unexpectedly, BI-VI was found to share a similar folding and disulfide bond connectivities not with cystatin superfamily inhibitors which inhibit the same cysteine proteinases but with the Bowman-Birk trypsin/chymotrypsin inhibitor from soybean (BBI-I). BBI-I is a 71-residue inhibitor which has two independent inhibitory sites toward the serine proteinases trypsin and chymotrypsin. These structural similarities with BBI-I suggest that they have evolved from a common ancestor and differentiated in function during a course of molecular evolution. | ||
- | + | Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean.,Hatano K, Kojima M, Tanokura M, Takahashi K Biochemistry. 1996 Apr 30;35(17):5379-84. PMID:8611527<ref>PMID:8611527</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | == | + | <div class="pdbe-citations 1bi6" style="background-color:#fffaf0;"></div> |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Ananas comosus]] | [[Category: Ananas comosus]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Hatano K-I]] |
Current revision
NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM
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