1dqc
From Proteopedia
(New page: 200px<br /><applet load="1dqc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqc" /> '''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMIC...) |
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| - | [[Image:1dqc.gif|left|200px]]<br /><applet load="1dqc" size=" | + | [[Image:1dqc.gif|left|200px]]<br /><applet load="1dqc" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION'''<br /> | '''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tachycitin, a 73-residue polypeptide having antimicrobial activity is | + | Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three-stranded beta-sheet and the latter a two-stranded beta-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process. |
==About this Structure== | ==About this Structure== | ||
| - | 1DQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: disulfide-rich]] | [[Category: disulfide-rich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:21 2008'' |
Revision as of 10:19, 21 February 2008
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SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION
Overview
Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three-stranded beta-sheet and the latter a two-stranded beta-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.
About this Structure
1DQC is a Single protein structure of sequence from Tachypleus tridentatus with as ligand. Full crystallographic information is available from OCA.
Reference
Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif., Suetake T, Tsuda S, Kawabata S, Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K, J Biol Chem. 2000 Jun 16;275(24):17929-32. PMID:10770921
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