期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 78, 期 10, 页码 2222-2237出版社
WILEY
DOI: 10.1002/prot.22734
关键词
signal recognition particle; correlation analysis; principal component analysis; overlap coefficient; protein targeting reaction; protein-protein interaction
资金
- NKBRSF [2007CB815202]
- NSFC [20721004, 20833008]
Signal recognition particle (SRP) and its receptor (SR) play essential role in the SRP-dependent protein targeting pathway. They interact with one another to precisely regulate the targeting reaction. The mechanism of this interaction consists of at least two discrete conformational states: complex formation and GTPase activation. Although structural studies have provided valuable insights into the understanding of the SRP-SR interaction, it still remains unclear that how SRP and SR GTPases use their intrinsic conformational flexibilities to exert multiple allosteric regulations on this interaction process. Here, we use computational simulations to present the dynamic behavior of the SRP GTPases at an atomic level to gain further understanding of SRP-SR interaction. We show that: (i) equilibrium conformational fluctuations contain a cooperative inter- and intradomain structural rearrangements that are functionally relevant to complex formation, (ii) a series of residues in different domains are identified to correlate with each other during conformational rearrangements, and (iii) alpha 3 and alpha 4 helices at domain interface actively rearrange their relative conformation to function as a bridge between the N domain and the core region of the G domain. These results, in addition to structural studies, would harness our understanding of the molecular mechanism for SRP and SR interaction. Proteins 2010; 78:2222-2237. (C) 2010 Wiley-Liss, Inc.
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