This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Molecular playground/beta 2 microglobulin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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 the protein associated with the formation of amyloid fibrils in DRA, a kidney disease.
+
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).
-
β-2 Microglobulin 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.
+
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>. 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.
+
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

Drag the structure with the mouse to rotate

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.

Proteopedia Page Contributors and Editors (what is this?)

Tyler Marcinko, Nick Borotto, David Canner, Michal Harel

Personal tools