1dqc
From Proteopedia
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'''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION''' | '''SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION''' | ||
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[[Category: Suetake, T.]] | [[Category: Suetake, T.]] | ||
[[Category: Tsuda, S.]] | [[Category: Tsuda, S.]] | ||
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Revision as of 11:09, 2 May 2008
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 Fri May 2 14:09:01 2008
