View source for 2bi6


==NMR STUDY OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM==
<StructureSection load='2bi6' size='340' side='right'caption='[[2bi6]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bi6]] 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=2BI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BI6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 18 models</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=2bi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bi6 OCA], [https://pdbe.org/2bi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bi6 RCSB], [https://www.ebi.ac.uk/pdbsum/2bi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bi6 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bi6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ananas comosus]]
[[Category: Large Structures]]
[[Category: Hatano K-I]]