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1dqc
From Proteopedia
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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 NH2 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
Page seeded by OCA on Sun Nov 25 03:31:20 2007
