Molecular playground/beta 2 microglobulin
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
<scene name='User:Nick_Borotto/Sandbox_1/Basic_view/3'>β-2 Microglobulin</scene> is a 12kd protein that self-assembles into amyloid fibrils in the presence of copper. This reaction is considered a likely cause for dialysis related amyloidosis; a disease where these fibrils build up in joints causing pain and eventually necessitating joint replacement. | <scene name='User:Nick_Borotto/Sandbox_1/Basic_view/3'>β-2 Microglobulin</scene> is a 12kd protein that self-assembles into amyloid fibrils in the presence of copper. This reaction is considered a likely cause for dialysis related amyloidosis; a disease where these fibrils build up in joints causing pain and eventually necessitating joint replacement. | ||
| - | The proposed mechanism for <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/1'>Dimer</scene> formation is that the copper binds near the N- | + | The proposed mechanism for <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/1'>Dimer</scene> formation is that the copper binds near the N-terminus of the protein, this binding causes structural shifts throughout, creating two new planes. These planes interact in an antiparallel fashion to form the dimer. |
Revision as of 03:57, 30 April 2010
|
is a 12kd protein that self-assembles into amyloid fibrils in the presence of copper. This reaction is considered a likely cause for dialysis related amyloidosis; a disease where these fibrils build up in joints causing pain and eventually necessitating joint replacement.
The proposed mechanism for formation is that the copper binds near the N-terminus of the protein, this binding causes structural shifts throughout, creating two new planes. These planes interact in an antiparallel fashion to form the dimer.
