Molecular playground/beta 2 microglobulin
From Proteopedia
| Line 1: | Line 1: | ||
<applet size='[450,338]' frame='true' align='right' | <applet size='[450,338]' frame='true' align='right' | ||
<caption='β-2 Microglobulin' scene='User:Nick_Borotto/Sandbox_1/Basic_view/4'/> | <caption='β-2 Microglobulin' scene='User:Nick_Borotto/Sandbox_1/Basic_view/4'/> | ||
| - | Banner: Beta-2 microglobulin | + | Banner: Beta-2 microglobulin is a 12 kDa protein sub-unit of the class I major histocompatibility complex, and in dialysis patients, it forms amyloid fibrils in a condition known as dialysis-related amyloidosis (DRA). |
| - | + | DRA is a complication of dialysis treatment in which these fibrils build up in joints causing pain and often eventually necessitating joint replacement. ?-2-microglobulin can self-assemble into amyloid fibrils under physiological conditions in vitro when copper is present. | |
| - | Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. | + | Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. Dimer formation is initiated when copper binds near the <scene name='User:Nick_Borotto/Sandbox_1/Metal_coordination_site/4'>N-terminus</scene>, copper binding causes structural changes 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 02:33, 2 May 2010
|
Banner: Beta-2 microglobulin is a 12 kDa protein sub-unit of the class I major histocompatibility complex, and in dialysis patients, it forms amyloid fibrils in a condition known as dialysis-related amyloidosis (DRA).
DRA is a complication of dialysis treatment in which these fibrils build up in joints causing pain and often eventually necessitating joint replacement. ?-2-microglobulin can self-assemble into amyloid fibrils under physiological conditions in vitro when copper is present.
Fibril assembly begins with the formation of a . Dimer formation is initiated when copper binds near the , copper binding causes structural changes throughout the protein, creating two new . These planes interact in an antiparallel fashion forming the dimer.
