This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ij2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ij2 |SIZE=350|CAPTION= <scene name='initialview01'>1ij2</scene>, resolution 1.70Å | |PDB= 1ij2 |SIZE=350|CAPTION= <scene name='initialview01'>1ij2</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ij2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ij2 OCA], [http://www.ebi.ac.uk/pdbsum/1ij2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ij2 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Kim, P S.]] | [[Category: Kim, P S.]] | ||
[[Category: Malashkevich, V N.]] | [[Category: Malashkevich, V N.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CD]] | ||
[[Category: gcn4 coiled coil]] | [[Category: gcn4 coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:30 2008'' |
Revision as of 18:20, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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 Sun Mar 30 21:20:30 2008
