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1ij1
From Proteopedia
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GCN4-pVLT Coiled-coil Trimer with Threonine at the d(12) 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
1IJ1 is a Single protein structure of sequence from [1] with and 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 Thu Feb 21 13:12:22 2008
Categories: Single protein | Akey, D L. | Kim, P S. | Malashkevich, V N. | ACE | ZN | Coiled coil | Gcn4
