1ij2
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ij2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ij2, resolution 1.70Å" /> '''GCN4-pVTL Coiled-coi...)
Next diff →
Revision as of 15:19, 20 November 2007
|
GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position
Overview
Coiled coils, estimated to constitute 3-5% of the encoded residues in most, genomes, are characterized by a heptad repeat, (abcdefg)(n), where the, buried a and d positions form the interface between multiple, alpha-helices. Although generally hydrophobic, a substantial fraction (, approximately 20%) of these a- and d-position residues are polar or, charged. We constructed variants of the well-characterized coiled coil, GCN4-p1 with a single polar residue (Asn, Gln, Ser, or Thr) at either an a, or a d position. The stability and oligomeric specificity of each variant, were measured, and crystal structures of coiled-coil trimers with, threonine or serine at either an a or a d position were determined. The, structures show how single polar residues in the interface affect not only, local packing, but also overall coiled-coil geometry as seen by changes in, the Crick supercoil parameters and core cavity volumes.
About this Structure
1IJ2 is a Single protein structure of sequence from [1] with CD and ACE as ligands. Full crystallographic information is available from OCA.
Reference
Buried polar residues in coiled-coil interfaces., Akey DL, Malashkevich VN, Kim PS, Biochemistry. 2001 May 29;40(21):6352-60. PMID:11371197
Page seeded by OCA on Tue Nov 20 17:26:20 2007
