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The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

Papaleo, E; Saladino, G; Lambrughi, M; Lindorff-Larsen, K; Gervasio, FL; Nussinov, R; (2016) The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery. Chemical Reviews 10.1021/acs.chemrev.5b00623. Green open access

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Abstract

Proteins are dynamic entities that undergo a plethora of conformational changes that may take place on a wide range of time scales. These changes can be as small as the rotation of one or a few side-chain dihedral angles or involve concerted motions in larger portions of the three-dimensional structure; both kinds of motions can be important for biological function and allostery. It is becoming increasingly evident that "connector regions" are important components of the dynamic personality of protein structures. These regions may be either disordered loops, i.e., poorly structured regions connecting secondary structural elements, or linkers that connect entire protein domains. Experimental and computational studies have, however, revealed that these regions are not mere connectors, and their role in allostery and conformational changes has been emerging in the last few decades. Here we provide a detailed overview of the structural properties and classification of loops and linkers, as well as a discussion of the main computational methods employed to investigate their function and dynamical properties. We also describe their importance for protein dynamics and allostery using as examples key proteins in cellular biology and human diseases such as kinases, ubiquitinating enzymes, and transcription factors.

Type: Article
Title: The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Open access status: An open access version is available from UCL Discovery
DOI: 10.1021/acs.chemrev.5b00623
Publisher version: http://dx.doi.org/10.1021/acs.chemrev.5b00623
Language: English
Additional information: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Chemical Reviews, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/acs.chemrev.5b00623.
UCL classification: UCL
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Chemistry
URI: https://discovery.ucl.ac.uk/id/eprint/1476099
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