期刊
BIOPHYSICAL CHEMISTRY
卷 104, 期 1, 页码 217-227出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0301-4622(02)00369-1
关键词
dimerization; G-protein coupled receptor; Monte Carlo; diffusion-limited aggregation; oligomerization
资金
- NIGMS NIH HHS [GM08353, T32 GM145304, R01 GM62930-01] Funding Source: Medline
Protein-protein dimerization is, ubiquitous in biology, but its role in self-organization remains unexplored. Here we use Monte Carlo simulations to demonstrate that under diffusion-limited conditions, reversible dimerization alone can cause membrane proteins to cluster into. oligomer-like structures. When multiple distinct protein species are able to form dimers, then heterodimerization and homodimerization can organize proteins into structured clusters that can affect cellular physiology. As an example, we demonstrate how receptor dimerization could provide a physical mechanism for regulating information flow by controlling receptor-receptor cross talk. These results are physically realistic for some membrane proteins, including members of the G-protein coupled receptor family, and may provide a physiological reason as to why many proteins dimerize. (C) 2003 Elsevier Science B.V. All rights reserved.
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