1pbz
From Proteopedia
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DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE
Overview
The structural characterization of de novo designed metalloproteins, together with determination of chemical reactivity can provide a detailed, understanding of the relationship between protein structure and functional, properties. Toward this goal, we have prepared a series of cyclic peptides, that bind to water-soluble metalloporphyrins (FeIII and CoIII). Neutral, and positively charged histidine-containing peptides bind with a high, affinity, whereas anionic peptides bind only weakly to the negatively, charged metalloporphyrin. Additionally, it was found that the peptide, becomes helical only in the presence of the metalloporphyrin. CD, experiments confirm that the metalloporphyrin binds specific cyclic, peptides with high affinity and with isodichroic behavior. Thermal, unfolding experiments show that the complex has "native-like" properties., Finally, NMR spectroscopy produced well dispersed spectra and experimental, restraints that provide a high-resolution solution structure of the, complexed peptide.
About this Structure
1PBZ is a Protein complex structure of sequences from [1] with ACE, NH2 and PC3 as ligands. Full crystallographic information is available from OCA.
Reference
De novo designed cyclic-peptide heme complexes., Rosenblatt MM, Wang J, Suslick KS, Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13140-5. Epub 2003 Oct 31. PMID:14595023
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