1dqc
From Proteopedia
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| - | [[Image:1dqc.gif|left|200px]] | + | [[Image:1dqc.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION''' | + | {{Structure |
| + | |PDB= 1dqc |SIZE=350|CAPTION= <scene name='initialview01'>1dqc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DQC is a [ | + | 1DQC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10770921 10770921] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tachypleus tridentatus]] | [[Category: Tachypleus tridentatus]] | ||
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[[Category: disulfide-rich]] | [[Category: disulfide-rich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:36 2008'' |
Revision as of 08:42, 20 March 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. 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
Page seeded by OCA on Thu Mar 20 10:42:36 2008
