2yxf: Difference between revisions

caption="2yxf, resolution 1.13Å" />

'''The high resolution crystal structure of beta2-microglobulin under physiological conditions'''<br />

==Overview==

beta(2)-Microglobulin (beta2-m), a light chain of the major, histocompatibility complex class I, forms amyloid fibrils in patients, undergoing long-term haemodialysis, causing dialysis-related amyloidosis., Based on a comparison of the X-ray structure obtained at pH 5.7 and that, of beta2-m in the histocompatibility complex, it has been proposed that, the continuous D-strand observed in the crystal structure at pH 5.7, increases the propensity of beta2-m to self-associate via edge-to-edge, interactions, thus initiating the formation of fibrils. To obtain further, insight into the mechanism by which amyloid fibrils form, we determined, the crystal structure of beta2-m at pH 7.0 at a resolution of up to 1.13, A. The crystal structure at pH 7.0 was basically the same as that at pH, 5.6, suggesting that the conversion of the beta-bulge in strand D into a, contiguous beta-strand is not unique to the crystals formed under slightly, acidic conditions. In other words, although the formation of beta2-m, fibrils was enhanced under acidic conditions, it remains unknown if it is, related to the increased propensity for the disappearance of the, beta-bulge in strand D. We consider that the enhanced fibrillation is more, directly coupled with the decreased stability leading to the increased, propensity of exposing amyloidogenic regions.

==About this Structure==

==Reference==

[[Category: immune system]]