C-JUN: Difference between revisions
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< | <StructureSection load='1jun' size='350' side='right' scene='' caption='Human C-Jun homodimer leucine zipper domain complex with acetyl (PDB code [[1jun]])'> | ||
== Introduction == | == Introduction == | ||
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== Structure Overview == | == Structure Overview == | ||
The structure of c-Jun is comprised of a leucine zipper as previously stated. This dimerization motif may be in one of two classes, both of which are required for DNA-binding transcription factors; the basic-domain leucine zipper proteins (bZIP) and the basic helix loop-helix-leucine zipper proteins(bHLH-ZIP) <ref name="two"> A Junius, F.K., Mackay, J.P., Bubb, W.A., Jensen, S.A., Weiss, A.S., King, G.F. 2006. Nuclear Magnetic Resonance Characterization of the Jun Leucine Zipper Domain: Unusual Properties of Coiled-Coil Interfacial Polar Residues?</ref>. The strand becomes an elongated coiled coil. This is formed by residues at the a and d positions in each of the two monomers, whereby they create hydrophobic centers which conform to the "knobs into holes" model by Crick. <ref name="two" />. Amino acids at these a and d positions are each surrounded by 4 additional residues from adjacent a-helix monomer <ref name="two" />. | The structure of c-Jun is comprised of a leucine zipper as previously stated. This dimerization motif may be in one of two classes, both of which are required for DNA-binding transcription factors; the basic-domain leucine zipper proteins (bZIP) and the basic helix loop-helix-leucine zipper proteins(bHLH-ZIP) <ref name="two"> A Junius, F.K., Mackay, J.P., Bubb, W.A., Jensen, S.A., Weiss, A.S., King, G.F. 2006. Nuclear Magnetic Resonance Characterization of the Jun Leucine Zipper Domain: Unusual Properties of Coiled-Coil Interfacial Polar Residues?</ref>. The strand becomes an elongated coiled coil. This is formed by residues at the a and d positions in each of the two monomers, whereby they create hydrophobic centers which conform to the "knobs into holes" model by Crick. <ref name="two" />. Amino acids at these a and d positions are each surrounded by 4 additional residues from adjacent a-helix monomer <ref name="two" />. | ||
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==Additional Resources== | ==Additional Resources== | ||
To See Additional information, see: [[Transcription and RNA Processing]] <br /> | To See Additional information, see: [[Transcription and RNA Processing]] <br /> | ||
</StructureSection> | |||
==3D structure of C-JUN== | ==3D structure of C-JUN== | ||
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[[1jun]] – hCJUN leucine zipper domain – human – NMR<br /> | [[1jun]] – hCJUN leucine zipper domain – human – NMR<br /> | ||
[[1jnm]] - hCJUN leucine zipper domain + DNA<br /> | [[1jnm]] - hCJUN leucine zipper domain + DNA<br /> | ||
[[1fos]] – hCJUN + p55 c-Fos + DNA | [[1fos]] – hCJUN + p55 c-Fos + DNA<br /> | ||
[[5fv8]] – hCJUN + FOSW<br /> | |||
== References == | == References == | ||