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1ij2
From Proteopedia
(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...) |
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| - | [[Image:1ij2.jpg|left|200px]]<br /><applet load="1ij2" size=" | + | [[Image:1ij2.jpg|left|200px]]<br /><applet load="1ij2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ij2, resolution 1.70Å" /> | caption="1ij2, resolution 1.70Å" /> | ||
'''GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position'''<br /> | '''GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coiled coils, estimated to constitute 3-5% of the encoded residues in most | + | 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== | ==About this Structure== | ||
| - | 1IJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CD and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371197 11371197] | Buried polar residues in coiled-coil interfaces., Akey DL, Malashkevich VN, Kim PS, Biochemistry. 2001 May 29;40(21):6352-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371197 11371197] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Akey, D | + | [[Category: Akey, D L.]] |
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Malashkevich, V | + | [[Category: Malashkevich, V N.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CD]] | [[Category: CD]] | ||
[[Category: gcn4 coiled coil]] | [[Category: gcn4 coiled coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:23 2008'' |
Revision as of 11:12, 21 February 2008
|
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 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 13:12:23 2008
