Transient association between proteins elicits alteration of dynamics at sites far away from interfaces

نویسندگان

چکیده

Summary Proteins are known to undergo structural changes upon binding partner proteins. However, the prevalence, extent, location, and function of change in protein dynamics due transient protein-protein interactions is not well documented. Here, we have analyzed a dataset 58 complexes three-dimensional structure structures their corresponding unbound forms evaluate induced by binding. Fifty-five percent cases showed significant away from interfaces. This always accompanied an observed change. Binding found alter inter-residue communication within tertiary about 90% cases. Also, residue motions accessible proteins form were maintained bound form. Further analyses revealed functional roles for distant site where was observed. Overall, results presented here strongly suggest that alteration commonly occurs.

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ژورنال

عنوان ژورنال: Structure

سال: 2021

ISSN: ['0969-2126', '1878-4186']

DOI: https://doi.org/10.1016/j.str.2020.11.015