期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 18, 页码 6963-6968出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0307567100
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资金
- NIGMS NIH HHS [R01 GM63536, R01 GM063536] Funding Source: Medline
The extracellular regions of adhesion proteins of the 1g superfamily comprise multiple, tandemly arranged domains. We used direct force measurements to investigate how this modular architecture contributes to the adhesive interactions of the neural cell adhesion molecule (NICAM), a representative of this protein class. The extracellular region of NCAM comprises five immunoglobulin and two fibronectin domains. Previous investigations generated different models for the mechanism of homophilic adhesion that each use different domains. We use force measurements to demonstrate that NCAM binds in two spatially distinct configurations. 1g-domain deletion mutants identified the domains responsible for each of the adhesive bonds. The measurements also confirmed the existence of a flexible hinge that alters the orientation of the adhesive complexes and the intermembrane distance. These results suggest that a combination of multiple bound states and internal molecular flexibility allows for sequentially synergistic bond formation and the ability to accommodate differences in intercellular space.
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