2bi6: Difference between revisions
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[[ | ==NMR STUDY OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM== | ||
<StructureSection load='2bi6' size='340' side='right' caption='[[2bi6]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bi6]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BI6 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bi6|1bi6]]</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=2bi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bi6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bi6 RCSB], [http://www.ebi.ac.uk/pdbsum/2bi6 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Ananas comosus]] | [[Category: Ananas comosus]] | ||
[[Category: Hatano, K I.]] | [[Category: Hatano, K I.]] | ||
[[Category: Cysteine protease inhibitor]] | [[Category: Cysteine protease inhibitor]] | ||
Revision as of 08:31, 8 October 2014
NMR STUDY OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM
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