Understanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding families

Martínez Herrerías, José Cristóbal; Castillo, Francisco; Ruiz Sanz, Javier; Murciano Calles, Javier; Cámara-Artigas, Ana; Luque Fernández, Irene

doi:https://doi.org/10.1016/BS.APCSB.2021.12.002

Capítulo aceptado (1.392Mo)

Identificadores

URI: https://hdl.handle.net/10481/99939

DOI: https://doi.org/10.1016/BS.APCSB.2021.12.002

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Editorial

Elsevier Inc.

Materia

EVH1 domains; GYF domains

Ligand design

Polyproline peptides

Protein-protein interactions

SH3 domains

Structure/function relationships in protein domains

UEV domains; WW domains

Date

2022-01-10

Referencia bibliográfica

Martinez JC, Castillo F, Ruiz-Sanz J, Murciano-Calles J, Camara-Artigas A, Luque I. Understanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding families. Adv Protein Chem Struct Biol. 2022;130:161-188. doi: 10.1016/bs.apcsb.2021.12.002. Epub 2022 Jan 10. PMID: 35534107.

Résumé

Within the modular protein domains there are five families that recognize proline-rich sequences: SH3, WW, EVH1, GYF and UEV domains. This chapter reviews the main strategies developed for the design of ligands for these families, including peptides, peptidomimetics and drugs. We also describe some studies aimed to understand the molecular reasons responsible for the intrinsic affinity and specificity of these domains.

Colecciones

DQF - Artículos

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