Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.

ABSTRACT: Symmetric protein dimers, trimers, and higher-order cyclic oligomers play key roles in many biological processes. However, structural studies of oligomeric systems by solution NMR can be difficult due to slow tumbling of the system and the difficulty in identifying NOE interactions across protein interfaces. Here, we present an automated method (RosettaOligomers) for determining the solution structures of oligomeric systems using only chemical shifts, sparse NOEs, and domain orientation restraints from residual dipolar couplings (RDCs) without a need for a previously determined structure of the monomeric subunit. The method integrates previously developed Rosetta protocols for solving the structures of monomeric proteins using sparse NMR data and for predicting the structures of both nonin

SUBMITTER: Sgourakis NG 

PROVIDER: S-EPMC3080108 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature