1ij2
From Proteopedia
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| - | [[Image:1ij2.jpg|left|200px]] | + | [[Image:1ij2.jpg|left|200px]] |
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| - | '''GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position''' | + | {{Structure |
| + | |PDB= 1ij2 |SIZE=350|CAPTION= <scene name='initialview01'>1ij2</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IJ2 is a [ | + | 1IJ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJ2 OCA]. |
==Reference== | ==Reference== | ||
| - | Buried polar residues in coiled-coil interfaces., Akey DL, Malashkevich VN, Kim PS, Biochemistry. 2001 May 29;40(21):6352-60. PMID:[http:// | + | Buried polar residues in coiled-coil interfaces., Akey DL, Malashkevich VN, Kim PS, Biochemistry. 2001 May 29;40(21):6352-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371197 11371197] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Akey, D L.]] | [[Category: Akey, D L.]] | ||
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[[Category: gcn4 coiled coil]] | [[Category: gcn4 coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:04 2008'' |
Revision as of 09:51, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | and | ||||||
| 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 Thu Mar 20 11:51:04 2008
