1bi6
From Proteopedia
(New page: 200px<br /><applet load="1bi6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bi6" /> '''NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM...) |
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| - | [[Image:1bi6.gif|left|200px]]<br /><applet load="1bi6" size=" | + | [[Image:1bi6.gif|left|200px]]<br /><applet load="1bi6" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM'''<br /> | '''NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bromelain inhibitor VI from pineapple stem (BI-VI) is a unique | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ananas_comosus Ananas comosus]. Full crystallographic information is available from [http:// | + | 1BI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ananas_comosus Ananas comosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BI6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ananas comosus]] | [[Category: Ananas comosus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hatano, K | + | [[Category: Hatano, K I.]] |
[[Category: cysteine protease inhibitor]] | [[Category: cysteine protease inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:33 2008'' |
Revision as of 09:55, 21 February 2008
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NMR STRUCTURE OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM
Overview
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.
About this Structure
1BI6 is a Protein complex structure of sequences from Ananas comosus. Full crystallographic information is available from OCA.
Reference
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
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