Odorant binding protein: Difference between revisions

Line 51:

'''Conformation transition mechanism:'''

The c-terminus of the protein bears mostly <scene name='68/683383/Hydrophobic_resid/1'>non-polar amino acids</scene>. Yet on the surface of the helix there are three exceptional amino acids: Asp-132, Glu-137, and Glu-141, which are conserved in moth PBP <ref>doi: 10.1016/j.bbrc.2005.07.176</ref>. Of these, residues <scene name='68/683383/Asp132/1'>Asp-132</scene> (and Glu-141, if present) triggers the formation of the alpha-helix upon protonation at low pH. This causes the <scene name='68/683383/~~1dqe_2fjy-bom~~/1'>ejaculation of the ligand from the binding pocket~~</scene>~~, which is replaced by the formatted alpha helix<ref>doi: 10.1016/j.bbrc</ref>.

The c-terminus of the protein bears mostly <scene name='68/683383/Hydrophobic_resid/1'>non-polar amino acids</scene>. Yet on the surface of the helix there are three exceptional amino acids: Asp-132, Glu-137, and Glu-141, which are conserved in moth PBP <ref>doi: 10.1016/j.bbrc.2005.07.176</ref>. Of these, residues <scene name='68/683383/Asp132/1'>Asp-132</scene> (and Glu-141, if present) triggers the formation of the alpha-helix upon protonation at low pH. This causes the transition from the <scene name='68/683383/B_form_with_ligand/1'>"A form"</scene>, to the <scene name='68/683383/A_form_with_ligand/1'>"B form"</scene> and the ejaculation of the ligand from the binding pocket, which is replaced by the formatted alpha helix<ref>doi: 10.1016/j.bbrc</ref>.

~~{{Button Toggle AnimationOnPause}}~~

Studies on other Lepidopterans that show a similar pH dependent conformation suggests that this model is a general model moth PBP<ref name="Leal" />.

Odorant binding protein: Difference between revisions

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@@ Line 51: / Line 51: @@
 '''Conformation transition mechanism:'''
-The c-terminus of the protein bears mostly <scene name='68/683383/Hydrophobic_resid/1'>non-polar amino acids</scene>. Yet on the surface of the helix there are three exceptional amino acids: Asp-132, Glu-137, and Glu-141, which are conserved in moth PBP <ref>doi: 10.1016/j.bbrc.2005.07.176</ref>. Of these, residues <scene name='68/683383/Asp132/1'>Asp-132</scene> (and Glu-141, if present) triggers the formation of the alpha-helix upon protonation at low pH. This causes the <scene name='68/683383/1dqe_2fjy-bom/1'>ejaculation of the ligand from the binding pocket</scene>, which is replaced by the formatted alpha helix<ref>doi: 10.1016/j.bbrc</ref>.
+The c-terminus of the protein bears mostly <scene name='68/683383/Hydrophobic_resid/1'>non-polar amino acids</scene>. Yet on the surface of the helix there are three exceptional amino acids: Asp-132, Glu-137, and Glu-141, which are conserved in moth PBP <ref>doi: 10.1016/j.bbrc.2005.07.176</ref>. Of these, residues <scene name='68/683383/Asp132/1'>Asp-132</scene> (and Glu-141, if present) triggers the formation of the alpha-helix upon protonation at low pH. This causes the transition from the <scene name='68/683383/B_form_with_ligand/1'>"A form"</scene>, to the <scene name='68/683383/A_form_with_ligand/1'>"B form"</scene> and the ejaculation of the ligand from the binding pocket, which is replaced by the formatted alpha helix<ref>doi: 10.1016/j.bbrc</ref>.
-{{Button Toggle AnimationOnPause}}
 Studies on other Lepidopterans that show a similar pH dependent conformation suggests that this model is a general model moth PBP<ref name="Leal" />.