|
|
Line 1: |
Line 1: |
| [[Image:1ij0.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1ij0.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1ij0| PDB=1ij0 | SCENE= }} | | {{STRUCTURE_1ij0| PDB=1ij0 | SCENE= }} |
|
| |
|
| '''Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position'''
| | ===Coiled Coil Trimer GCN4-pVLS Ser at Buried D 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11371197}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11371197 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_11371197}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
Line 25: |
Line 29: |
| [[Category: Malashkevich, V N.]] | | [[Category: Malashkevich, V N.]] |
| [[Category: Coiled coil trimer]] | | [[Category: Coiled coil trimer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:03:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:18:17 2008'' |