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Protein Interaction Domains and Post-Translational Modifications: Structural Features and Drug Discovery Applications.

Abstract：

BACKGROUND:Many pathways regarding healthy cells and/or linked to diseases onset and progression depend on large assemblies including multi-protein complexes. Protein-protein interactions may occur through a vast array of modules known as Protein Interaction Domains (PIDs). OBJECTIVE:This review concerns with PIDs recognizing post-translationally modified peptide sequences and intends to provide the scientific community with state of art knowledge on their 3D structures, binding topologies and potential applications in the drug discovery field. METHOD:Several databases, such as the Pfam (Protein family), the SMART (Simple Modular Architecture Research Tool) and the PDB (Protein Data Bank), were searched to look for different domain families and gain structural information on protein complexes in which particular PIDs are involved. Recent literature on PIDs and related drug discovery campaigns were retrieved through Pubmed and analyzed. RESULTS AND CONCLUSION:PIDs are rather versatile as concerned with their binding preferences. Many of them recognize specifically only determined amino acid stretches with post-translational modifications, a few others are able to interact with several post-translationally modified sequences or with unmodified ones. Many PIDs can be linked to different diseases including cancer. The tremendous amount of available structural data led to the structure-based design of several molecules targeting protein-protein interactions mediated by PIDs, including peptides, peptidomimetics and small compounds. More studies are needed to fully role out, among different families, PIDs that can be considered reliable therapeutic targets, however, attacking PIDs rather than catalytic domains of a particular protein may represent a route to obtain selective inhibitors.

journal_name

Curr Med Chem

journal_title

Current medicinal chemistry

authors

Vincenzi M,Mercurio FA,Leone M

doi

10.2174/0929867326666190620101637

subject

Has Abstract

pub_date

2020-01-01 00:00:00

pages

6306-6355

issue

eissn

0929-8673

issn

1875-533X

pii

CMC-EPUB-99083

journal_volume

pub_type

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Protein Interaction Domains and Post-Translational Modifications: Structural Features and Drug Discovery Applications.