1qgm
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(New page: 200px<br /><applet load="1qgm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgm" /> '''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO...)
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Revision as of 22:33, 20 November 2007
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THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.
Overview
Upon air oxidation, a peptide corresponding to the 30-residue N-terminal, subdomain of carp granulin-1 spontaneously formed the disulfide pairing, observed in the native protein. Structural characterization using NMR, showed the presence of a defined secondary structure within this peptide., The chemical shifts for most of the alphaCH protons of the peptide and the, protein are very similar, and the observed NOE contacts of the peptide, strongly resemble those in the protein. A structure calculation of the, peptide using NOE distance constraints indicates that the peptide fragment, adopts the same conformation as formed within the native protein. The, 30-residue N-terminal peptide of carp granulin-1 is the first example of, an independently folded stack of two beta-hairpins reinforced by two, interhairpin disulfide bonds. Two key areas of the structure show a, clustering of hydrophobic residues that may account for its exceptional, conformational stability.
About this Structure
1QGM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein., Vranken WF, Chen ZG, Xu P, James S, Bennett HP, Ni F, J Pept Res. 1999 May;53(5):590-7. PMID:10424355
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