Amyloid beta: Difference between revisions
Laura Olney (talk | contribs) No edit summary |
Laura Olney (talk | contribs) No edit summary |
||
| Line 4: | Line 4: | ||
==Structure== | ==Structure== | ||
Amyoloid beta is actually the <scene name='Amyloid_beta/C-term/1'>C-terminal</scene> of the <scene name='Amyloid_beta/App/1'>Amyloid Precursor Protein</scene> which is a type I membrane-spanning glycoprotein encoded on chromosome 21 [[http://proteopedia.org/wiki/index.php/Amyloid_precursor_protein APP]].<ref name="alz" /> Amyloid beta results from an abnormal cleavage by [http://proteopedia.org/wiki/index.php/Beta_secretase beta-secretase] at the N-terminal and gamma-secretase at the C-terminal[[http://en.wikipedia.org/wiki/Beta_amyloid]]. The cleavage is nonspecific and results in peptides 39-43 amino acids in length, with 42 being the most common. Such cleavages occur most commonly in the plasma membrane | Amyoloid beta is actually the <scene name='Amyloid_beta/C-term/1'>C-terminal</scene> of the <scene name='Amyloid_beta/App/1'>Amyloid Precursor Protein</scene> which is a type I membrane-spanning glycoprotein encoded on chromosome 21 [[http://proteopedia.org/wiki/index.php/Amyloid_precursor_protein APP]].<ref name="alz" /> Amyloid beta results from an abnormal cleavage by [http://proteopedia.org/wiki/index.php/Beta_secretase beta-secretase] at the N-terminal and gamma-secretase at the C-terminal[[http://en.wikipedia.org/wiki/Beta_amyloid]]. The cleavage is nonspecific and results in peptides 39-43 amino acids in length, with 42 being the most common. Such cleavages occur most commonly in the plasma membrane though it can also occur in neuronal membranes.<ref name="alz" /> | ||
The first 16 residues, Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu--Val-His-His-Gln-Lys, are mostly hydrophobic while <scene name='Amyloid_beta/Cu/1'>His13 and His14</scene> form a binding domain for Cu(II). Residues 12-23 function as the <scene name='Amyloid_beta/Self/1'>self recognition</scene> region allowing for the formation of dimers and/or oligomers. This region also serves as the binding site for cholesterol, apolipoproteinE, alpha7nAChr, and amyloid beta-peptide binding alcohol dehydrogenase.<ref name="alz" /> | The first 16 residues, Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu--Val-His-His-Gln-Lys, are mostly hydrophobic while <scene name='Amyloid_beta/Cu/1'>His13 and His14</scene> form a binding domain for Cu(II). Residues 12-23 function as the <scene name='Amyloid_beta/Self/1'>self recognition</scene> region allowing for the formation of dimers and/or oligomers. This region also serves as the binding site for cholesterol, apolipoproteinE, alpha7nAChr, and amyloid beta-peptide binding alcohol dehydrogenase.<ref name="alz" /> | ||