Tyler marcinko/sandbox 1
From Proteopedia
| Line 14: | Line 14: | ||
== B2m Mutations == | == B2m Mutations == | ||
| - | There have been several mutants of B2m generated that have been essential in defining some of the early molecular events that ultimately lead to amyloidosis. | + | There have been several mutants of B2m generated that have been essential in defining some of the early molecular events that ultimately lead to amyloidosis. The <scene name='60/609778/H31f/1'>H31F mutant</scene> form of B2m has permitted the crystal structure of the hexamer be solved. However, this mutant of B2m does not progress to form amyloid fibrils and instead forms off-pathway oligomers. |
| + | |||
| + | Another important variant of B2m is | ||
Structural effects of the various mutations and their oligomers | Structural effects of the various mutations and their oligomers | ||
Revision as of 20:55, 29 November 2014
|
Contents |
Beta-2-microglobulin
Beta-2 microglobulin (B2m) is a structural protein sub-unit of the class I major histocompatibility complex. It has a molecular weight of approximately 12 kDa. In dialysis patients, it has the propensity to form amyloid fibrils in a condition known as dialysis-related amyloidosis (DRA). The mechanism of oligomerization and eventual fibrillation are of particular interest to the Vachet Research Group at the University of Massachusetts-Amherst.
Disease
Aggregation Mechanism
There are several processes that can cause B2m to aggregate and ultimately form amyloid fibrils (citations). In the copper-catalyzed pathway, the process begins with the formation of a homodimer. Dimer formation is initiated when copper binds near the . Copper binding causes structural changes throughout the protein creating two new planes. These planes interact in an antiparallel fashion which forms the basis of the non-covalent .
Soluble oligomers then undergo higher order assembly steps to form larger structures. Evidence for the tetramer and hexamer have been measured using a variety of different analytical methods. Notably,
B2m Mutations
There have been several mutants of B2m generated that have been essential in defining some of the early molecular events that ultimately lead to amyloidosis. The form of B2m has permitted the crystal structure of the hexamer be solved. However, this mutant of B2m does not progress to form amyloid fibrils and instead forms off-pathway oligomers.
Another important variant of B2m is
Structural effects of the various mutations and their oligomers
Code to color a green scene
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
Useful Links
The Vachet Lab [1]
