作者: G P Manjunath , Praveena L Ramanujam , Sanjeev Galande
DOI: 10.1007/S12038-017-9727-0
关键词: Computational biology 、 Multiple sequence alignment 、 Peptide binding 、 Plasma protein binding 、 Peptide sequence 、 Scaffold protein 、 Sequence alignment 、 Conserved sequence 、 PDZ domain 、 Chemistry
摘要: Protein scaffolds as essential backbones for organization of supramolecular signalling complexes are a recurrent theme in several model systems. Scaffold proteins preferentially employ linear peptide binding motifs recruiting their interaction partners. PDZ domains one the more commonly encountered including those involved scaffolding functions. This domain is known its promiscuity both terms ligand selection, mode with ligands well association other protein domains. subject to means regulations by virtue functional diversity. Additionally, refractive effect mutations and maintain three-dimensional architecture under extreme mutational load. The biochemical biophysical basis this selectivity has been investigated reviewed extensively. present review focuses on plasticity inherent implications modular evolution cellular pathways higher eukaryotes.