1zim
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(New page: 200px<br /><applet load="1zim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zim, resolution 2.00Å" /> '''GCN4-LEUCINE ZIPPER ...)
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Revision as of 05:21, 21 November 2007
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GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE TRIMERIC STATE
Overview
A conserved asparagine (Asn 16) buried in the interface of the GCN4, leucine zipper selectively favours the parallel, dimeric, coiled-coil, structure. To test if other polar residues confer oligomerization, specificity, the structural effects of Gln and Lys substitutions for Asn, 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant, formed exclusively dimers. In contrast, Gln 16, despite its chemical, similarity to Asn, allowed the peptide to form both dimers and trimers., The Gln 16 side chain was accommodated by qualitatively different, interactions in the dimer and trimer crystal structures. These findings, demonstrate that the structural selectivity of polar residues results not, only from the burial of polar atoms, but also depends on the, complementarity of the side-chain stereochemistry with the surrounding, structural environment.
About this Structure
1ZIM is a Single protein structure of sequence from Saccharomyces cerevisiae with ACE as ligand. Full crystallographic information is available from OCA.
Reference
Buried polar residues and structural specificity in the GCN4 leucine zipper., Gonzalez L Jr, Woolfson DN, Alber T, Nat Struct Biol. 1996 Dec;3(12):1011-8. PMID:8946854
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