NMR observable-based structure refinement of DAP12-NKG2C activating immunoreceptor complex in explicit membranes.

ABSTRACT: NMR observables, such as NOE-based distance measurements, are increasingly being used to characterize membrane protein structures. However, challenges in membrane protein NMR studies often yield a relatively small number of such restraints that can create ambiguities in defining critical side chain-side chain interactions. In the recent solution NMR structure of the DAP12-NKG2C immunoreceptor transmembrane helix complex, five functionally required interfacial residues (two Asps and two Thrs in the DAP12 dimer and one Lys in NKG2C) display a surprising arrangement in which one Asp side chain faces the membrane hydrophobic core. To explore whether these side-chain interactions are energetically optimal, we used the published distance restraints for molecular dynamics simulations in explicit

SUBMITTER: Cheng X 

PROVIDER: S-EPMC3318141 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature