1zpx
From Proteopedia
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NMR Structure of Mcol1-[13-33] from Hydra
Overview
Synthetic replicates of naturally occurring cysteine-rich peptides such as, hormones, neurotransmitters, growth factors, enzyme inhibitors, defensins, and toxins often can be oxidatively folded in high yields to their native, structure in simple redox buffers. Thereby, identical cysteine patterns in, the sequence were found to generate identical disulfide connectivities and, homologous spatial structures despite significant variability in the, non-cysteine positions. Minicollagen-1 from the nematocysts of Hydra is a, trimeric protein that contains cysteine-rich domains at the N and C, termini, which are involved in the assembly of an intermolecular disulfide, network. Determination of the three-dimensional structures of peptides, corresponding to the N-terminal and C-terminal domains by NMR spectroscopy, revealed a remarkable exception from the general rule. Despite an, identical cysteine pattern, the two domains of minicollagen-1 form, different disulfide bridges and exhibit distinctly different folds, both, of which are not found in the current structural databases. To our, knowledge, this is the first case where two relatively short peptides with, the abundant cysteine residues in identical sequence positions fold, uniquely and with high yields into defined, but differing, structures., Therefore, the cysteine-rich domains of minicollagen constitute ideal, model systems for studies of the interplay between folding and oxidation, in proteins.
About this Structure
1ZPX is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
The two cysteine-rich head domains of minicollagen from Hydra nematocysts differ in their cystine framework and overall fold despite an identical cysteine sequence pattern., Milbradt AG, Boulegue C, Moroder L, Renner C, J Mol Biol. 2005 Dec 2;354(3):591-600. Epub 2005 Oct 14. PMID:16257007
Page seeded by OCA on Tue Jan 29 17:40:27 2008
