1sop
From Proteopedia
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C-terminal cystine-rich domain of Minicollagen-I from Hydra
Overview
The minicollagens found in the nematocysts of Hydra constitute a family of, invertebrate collagens with unusual properties. They share a common, modular architecture with a central collagen sequence ranging from 14 to, 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and, short terminal domains that show a conserved cysteine pattern, (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed, to function in a switch of the disulfide connectivity from intra- to, intermolecular bonds during maturation of the capsule wall. The solution, structure of the C-terminal fragment including a minicollagen, cysteine-rich domain of minicollagen-1 was determined in two independent, groups by 1H NMR. The corresponding peptide comprising the last 24, residues of the molecule was produced synthetically and refolded by, oxidation under low protein concentrations. Both presented structures are, identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to, serve as the polymerization module of the nematocyst capsule.
About this Structure
1SOP is a Single protein structure of sequence from [1] with ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall., Pokidysheva E, Milbradt AG, Meier S, Renner C, Haussinger D, Bachinger HP, Moroder L, Grzesiek S, Holstein TW, Ozbek S, Engel J, J Biol Chem. 2004 Jul 16;279(29):30395-401. Epub 2004 May 3. PMID:15123641
Page seeded by OCA on Sun Nov 25 00:54:36 2007
