C-JUN: Difference between revisions

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[[Image:1jun.png|left|thumb|''Figure 1.'' A 3-D representation of the two alpha helices which form a coiled coil [http://www.rcsb.org/pdb/explore/jmol.do?structureId=1JUN] ]]

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"/>.

The a and d residues each exhibit varying types of packing in terms of this "knobs into holes" theory. According to Harbury et al.(24) the leucines at the a positions are packed "parallel" in such a way that the C-alpha-C-beta bond vector lies in a parallel manner to the C-alpha-C-alpha vector at the base of the acceptor hole on adjacent helix <ref name="one">. Whereas the opposite is true for the leucines in the d positions. Here the residues are packed in a "perpendicular" nature <ref name="one">. The bond vector of the C-alpha-C-beta pack approximately perpendicular to the C-alpha-C-alpha vector at the base of the hole of the second helix in which it packs <ref name="one">. Therefore only the leucine side chains in the a positions, which point away from the boundary, make van der Waals interactions <ref name="one">.

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@@ Line 17: / Line 17: @@
 [[Image:1jun.png|left|thumb|''Figure 1.'' A 3-D representation of the two alpha helices which form a coiled coil [http://www.rcsb.org/pdb/explore/jmol.do?structureId=1JUN] ]]
-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"/>.
 The a and d residues each exhibit varying types of packing in terms of this "knobs into holes" theory.  According to Harbury et al.(24) the leucines at the a positions are packed "parallel" in such a way that the C-alpha-C-beta bond vector lies in a parallel manner to the C-alpha-C-alpha vector at the base of the acceptor hole on adjacent helix <ref name="one">.  Whereas the opposite is true for the leucines in the d positions.  Here the residues are packed in a "perpendicular" nature <ref name="one">.  The bond vector of the C-alpha-C-beta pack approximately perpendicular to the C-alpha-C-alpha vector at the base of the hole of the second helix in which it packs <ref name="one">.  Therefore only the leucine side chains in the a positions, which point away from the boundary, make van der Waals interactions <ref name="one">.