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The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall

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 termina...

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Bibliographic Details
Main Authors: Pokidysheva, Elena (Author) , Holstein, Thomas W. (Author) , Özbek, Suat (Author)
Format: Article (Journal)
Language:English
Published: July 16, 2004
In: The journal of biological chemistry
Year: 2004, Volume: 279, Issue: 29, Pages: 30395-30401
ISSN:1083-351X
DOI:10.1074/jbc.M403734200
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1074/jbc.M403734200
Verlag, kostenfrei, Volltext: http://www.jbc.org/content/279/29/30395
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Author Notes:Elena Pokidysheva, Alexander G. Milbradt, Sebastian Meier, Christian Renner, Daniel Häussinger, Hans Peter Bächinger, Luis Moroder, Stephan Grzesiek, Thomas W. Holstein, Suat Özbek, and Jürgen Engel
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Summary: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.
Item Description:Gesehen am 08.05.2017
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M403734200

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