Molecular playground/beta 2 microglobulin
From Proteopedia
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<scene name='User:Nick_Borotto/Sandbox_1/Basic_view/4'>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/4'>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. | ||
| - | Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. This structures formation is initiated when copper binds near the <scene name='User:Nick_Borotto/Sandbox_1/Metal_coordination_site/ | + | Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. This structures formation is initiated when copper binds near the <scene name='User:Nick_Borotto/Sandbox_1/Metal_coordination_site/4'>N-terminus</scene>, this binding causes structural shifts throughout the protein, creating two new <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_interface/4'>planes</scene>. These planes interact in an antiparallel fashion forming the dimer. |
Revision as of 05:19, 30 April 2010
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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.
Fibril assembly begins with the formation of a . This structures formation is initiated when copper binds near the , this binding causes structural shifts throughout the protein, creating two new . These planes interact in an antiparallel fashion forming the dimer.
