1bi6

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[[Image:1bi6.png|left|200px]]
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==NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM==
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<StructureSection load='1bi6' size='340' side='right' caption='[[1bi6]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bi6]] 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=1BI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BI6 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bi6|2bi6]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bi6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bi6 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1bi6| PDB=1bi6 | SCENE= }}
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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>
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===NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_8611527}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1bi6]] 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=1BI6 OCA].
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</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 09:42, 13 August 2014

NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM

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