Self‐assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations
Citations Over Time
Abstract
The Sarcolipin (SLN) is a single trans-membrane protein that can self-assembly to dimer and oligomer for playing importantphysiological function. In this work, we addressed the dimerization of wild type SLN (wSLN) and its mutants (mSLNs) - I17A and I20A, using both coarse-grained (CG) and atomistic (AT) molecular dynamics (MD) simulations. Our results demonstrated that wSLN homodimer assembled as a left-handed helical complex, while mSLNs heterodimers assembled as right-handed complexes. Analysis of residue-residue contacts map indicated that isoleucine (Ile)-leucione (Leu) zipper domain played an important role in dimerization. The potential of mean force (PMF) demonstrated that wSLN homodimer was more stable than mSLNs heterodimers. Meanwhile, the mSLNs heterodimers preferred right-handed rather than left-handed helix. AT-MD simulations for wSLN and mSLNs were also in line with CG-MD simulations. These results provided the insights for understanding the mechanisms of SLNs self-assembling. Proteins 2017; 85:1065-1077. © 2017 Wiley Periodicals, Inc.
Related Papers
- → Hydrophobic cavity in C-terminus is essential for hTNF-α trimer conformation(2012)13 cited
- → ESR detection of non-equivalent scandium trimer(1994)15 cited
- → Results and discussion(2015)3 cited
- → Phenoxyaluminium compounds(1978)10 cited
- → Influence of trimer water cluster in liquid materials on conduction phenomena by using nano-second pulse(2002)