1ij0: Difference between revisions

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New page: left|200px<br /><applet load="1ij0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ij0, resolution 1.86Å" /> '''Coiled Coil Trimer G...
 
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[[Image:1ij0.jpg|left|200px]]<br /><applet load="1ij0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ij0.jpg|left|200px]]<br /><applet load="1ij0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ij0, resolution 1.86&Aring;" />
caption="1ij0, resolution 1.86&Aring;" />
'''Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position'''<br />
'''Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position'''<br />


==Overview==
==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.
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==
1IJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IJ0 OCA].  
1IJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</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=1IJ0 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.L.]]
[[Category: Akey, D L.]]
[[Category: Kim, P.S.]]
[[Category: Kim, P S.]]
[[Category: Malashkevich, V.N.]]
[[Category: Malashkevich, V N.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: coiled coil trimer]]
[[Category: coiled coil trimer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:26:11 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:22 2008''

Revision as of 14:12, 21 February 2008

File:1ij0.jpg


1ij0, resolution 1.86Å

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Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position

OverviewOverview

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 StructureAbout this Structure

1IJ0 is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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