Conformational Changes Induced by S34Y and R98C Variants in the Death Domain of Myd88.

ABSTRACT: Myeloid differentiating factor 88 (Myd88) is a universal adaptor protein that plays a critical role in innate immunity by mediating TLR downstream signaling. Myd88 death domain (DD) forms an oligomeric complex by association with other DD-containing proteins such as IRAK4. Despite its universal role, polymorphisms in Myd88 can result in several diseases. Previous studies have suggested that, out of several non-synonymous single-nucleotide polymorphisms (nsSNPs), the variants S34Y and R98C in the DD of Myd88 disrupt the formation of the Myddosome complex. Therefore, we performed molecular dynamics (MD) simulations on wild-type (Myd88^WT) and mutant (Myd88^S34Y, Myd88^R98C) DDs to evaluate the subtle conformational changes induced by these mutations. Our results

SUBMITTER: Gosu V 

PROVIDER: S-EPMC7106778 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature