期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 16, 页码 6450-6455出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1019051108
关键词
EPR spectroscopy; fluorescence spectroscopy; molecular recognition; protein targeting; GTPases
资金
- National Institutes of Health [GM078024, GM068041]
- DARPA Protein Design Processes
- Burroughs Welcome Foundation
- Henry and Camille Dreyfus Foundation
- Arnold and Mabel Beckman Foundation
- David and Lucile Packard Foundation
- Grants-in-Aid for Scientific Research [23687022] Funding Source: KAKEN
Interactions between proteins underlie numerous biological functions. Theoretical work suggests that protein interactions initiate with formation of transient intermediates that subsequently relax to specific, stable complexes. However, the nature and roles of these transient intermediates have remained elusive. Here, we characterized the global structure, dynamics, and stability of a transient, on-pathway intermediate during complex assembly between the Signal Recognition Particle (SRP) and its receptor. We show that this intermediate has overlapping but distinct interaction interfaces from that of the final complex, and it is stabilized by long-range electrostatic interactions. A wide distribution of conformations is explored by the intermediate; this distribution becomes more restricted in the final complex and is further regulated by the cargo of SRP. These results suggest a funnel-shaped energy landscape for protein interactions, and they provide a framework for understanding the role of transient intermediates in protein assembly and biological regulation.
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