Odorant binding protein: Difference between revisions
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Nurit Eliash (talk | contribs) No edit summary |
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'''Conformation transition mechanism:''' | '''Conformation transition mechanism:''' | ||
The c-terminus of the protein bears mostly non-polar amino acids. 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 <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>. | ||
{{Button Toggle AnimationOnPause}} | {{Button Toggle AnimationOnPause}} | ||
