1ij0: Difference between revisions

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[[Image:1ij0.png|left|200px]]
==Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position==
<StructureSection load='1ij0' size='340' side='right' caption='[[1ij0]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ij0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IJ0 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ij0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ij0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ij0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ij0 PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1ij0|  PDB=1ij0  |  SCENE=  }}
Buried polar residues in coiled-coil interfaces.,Akey DL, Malashkevich VN, Kim PS Biochemistry. 2001 May 29;40(21):6352-60. PMID:11371197<ref>PMID:11371197</ref>


===Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


{{ABSTRACT_PUBMED_11371197}}
==See Also==
 
*[[Gcn4|Gcn4]]
==About this Structure==
== References ==
[[1ij0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJ0 OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:011371197</ref><references group="xtra"/>
[[Category: Akey, D L.]]
[[Category: Akey, D L.]]
[[Category: Kim, P S.]]
[[Category: Kim, P S.]]

Revision as of 08:31, 8 June 2014

Coiled Coil Trimer GCN4-pVLS Ser at Buried D PositionCoiled Coil Trimer GCN4-pVLS Ser at Buried D Position

Structural highlights

1ij0 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

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.

Buried polar residues in coiled-coil interfaces.,Akey DL, Malashkevich VN, Kim PS Biochemistry. 2001 May 29;40(21):6352-60. PMID:11371197[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Akey DL, Malashkevich VN, Kim PS. Buried polar residues in coiled-coil interfaces. Biochemistry. 2001 May 29;40(21):6352-60. PMID:11371197

1ij0, resolution 1.86Å

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