1t1v
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(New page: 200px<br /><applet load="1t1v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1v, resolution 1.60Å" /> '''Crystal Structure of...)
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Revision as of 00:48, 21 November 2007
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Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution
Overview
We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a, member of a new mammalian protein family of unknown function. The observed, "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of, glutaredoxins, even in the N-terminal region where the sequence similarity, between the two protein families is negligible. In particular, SH3BGRL3, displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The, loop hosts a six residue insertion, yielding an extra N-terminal-capped, helical turn, first observed here for the thioredoxin fold. This, together, with deletion of both Cys residues, results in a substantial reshaping of, the neighboring cleft, where glutathione is hosted in glutaredoxins. While, not active in redox reaction and glutathione binding, SH3BGRL3 may act as, an endogenous modulator of glutaredoxin activities by competing, with its, fully conserved thioredoxin fold, for binding to yet unknown target, proteins.
About this Structure
1T1V is a Single protein structure of sequence from Mus musculus with SO4, ACY and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution., Nardini M, Mazzocco M, Massaro A, Maffei M, Vergano A, Donadini A, Scartezzini P, Bolognesi M, Biochem Biophys Res Commun. 2004 May 28;318(2):470-6. PMID:15120624
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