Single versus dual-binding conformations in cellulosomal cohesin–dockerin complexes

Nash, Michael A. and Smith, Steven P. and Fontes, Carlos Mga and Bayer, Edward A.. (2016) Single versus dual-binding conformations in cellulosomal cohesin–dockerin complexes. Current Opinion in Structural Biology, 40. pp. 89-96.

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Official URL: http://edoc.unibas.ch/51754/

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Cohesins and dockerins are complementary interacting protein modules that form stable and highly specific receptor-ligand complexes. They play a crucial role in the assembly of cellulose-degrading multi-enzyme complexes called cellulosomes and have potential applicability in several technology areas, including biomass conversion processes. Here, we describe several exceptional properties of cohesin-dockerin complexes, including their tenacious biochemical affinity, remarkably high mechanostability and a dual-binding mode of recognition that is contrary to the conventional lock-and-key model of receptor-ligand interactions. We focus on structural aspects of the dual mode of cohesin-dockerin binding, highlighting recent single-molecule analysis techniques for its explicit characterization.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Synthetic Systems (Nash)
UniBasel Contributors:Nash, Michael
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Jun 2017 07:41
Deposited On:14 Jun 2017 07:41

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