2b1f: Difference between revisions

Revision as of 18:52, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b1f.png

Template:STRUCTURE 2b1f

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeatAntiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat

Template:ABSTRACT PUBMED 16472744

About this StructureAbout this Structure

2B1F is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat., Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M, Structure. 2006 Feb;14(2):247-55. PMID:16472744

Page seeded by OCA on Sun Jul 27 18:52:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2b1f.gif|left|200px]]
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-'''Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat'''
+===Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat===
-==Overview==
+<!--
-Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with nonpolar side chains at the first (a) and fourth (d) positions. We investigate here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at the a, d, and g positions in determining the structures of coiled coils using mutants of the GCN4 leucine zipper dimerization domain. When three charged residues at the g positions in the parental sequence are replaced by nonpolar alanine or valine side chains, stable four-helix structures result. The X-ray crystal structures of the tetramers reveal antiparallel, four-stranded coiled coils in which the a, d, and g side chains interlock in a combination of knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the canonical 3-4 heptad repeat. The results suggest that the conserved, charged residues at the g positions in the GCN4 leucine zipper can impart a negative design element to disfavor thermodynamically more stable, antiparallel tetramers.
+The line below this paragraph, {{ABSTRACT_PUBMED_16472744}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16472744 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16472744}}
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 [[Category: Protein design]]
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