The potential impact of recent developments in three-dimensional quantitative interaction proteomics on structural biology

Nurcan Tuncbag, Attila Gursoy, Ozlem Keskin, Ruth Nussinov
<span title="2016-05-03">2016</span> <i title="Informa UK Limited"> <a target="_blank" rel="noopener" href="" style="color: black;">Espert Review of Proteomics</a> </i> &nbsp;
Keywords integrative modeling; structural bioinformatics; assembly modeling; protein interactions In the cell, proteins are not isolated entities. They interact with each other and with other molecules including DNA, RNA, small ligands, and membrane lipids to carry out their functions. They typically form multimeric assemblies through non-covalent interactions; examples include the nucleosome, ribosome, viral coats, the E2/E3 ubiquitination machinery, the Mediator, membrane-anchored
more &raquo; ... and more. The strength of the non-covalent interactions and the life times of the assemblies vary in the cell and the spatial organization of their so-called 'interactomes' reflects a temporal and dynamic behavior. Some interactions are elicited by specific regulatory states; others take place in distinct cellular compartments or spatial locations. Some are long-others are short-lived regulating intracellular signaling bursts. Capturing these transient interactions with conventional techniques is challenging. In addition, some proteins interact with their partners following post-translational modification events such as phosphorylation, ubiquitination, methylation, or hydroxylation of specific residues. Abnormal alterations in protein interactions can cause cancer, neurodegenerative diseases and other pathologies. The ultimate goal in structural biology is to reveal the three dimensional interaction details of proteins which are essential in order to understand how cellular function is carried out. The characteristics of proteinprotein interactions and their physicochemical properties is reviewed extensively in [1].
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="">doi:10.1080/14789450.2016.1182023</a> <a target="_blank" rel="external noopener" href="">pmid:27104235</a> <a target="_blank" rel="external noopener" href="">pmcid:PMC4938151</a> <a target="_blank" rel="external noopener" href="">fatcat:l7n5kjtpnje4pcx7zmhxqkv75m</a> </span>
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