Structural Diversity in Calmodulin - Peptide Interactions

被引：10

作者：

Durvanger, Zsolt ^{[1
]}

Harmat, Veronika ^{[1
,2
]}

机构：

[1] Eotvos Lorand Univ, Inst Chem, Lab Struct Chem & Biol, Pazmany Peter Setany 1-A, H-1117 Budapest, Hungary

[2] MTA ELTE Prot Modelling Res Grp, Budapest, Hungary

来源：

CURRENT PROTEIN & PEPTIDE SCIENCE | 2019年 / 20卷 / 11期

基金：

匈牙利科学研究基金会;

关键词：

Calcium; calmodulin; EF-hands; calmodulin-peptide complexes; protein-peptide interaction; binding motifs; NITRIC-OXIDE SYNTHASE; DEPENDENT PROTEIN-KINASE; CHEMICAL CROSS-LINKING; IQ-MOTIF; CRYSTAL-STRUCTURE; TARGET PEPTIDE; BINDING DOMAIN; CALCIUM; COMPLEX; INSIGHTS;

D O I：

10.2174/1389203720666190925101937

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calmodulin (CaM) is a highly conserved eukaryotic Ca2+ sensor protein that is able to bind a large variety of target sequences without a defined consensus sequence. The recognition of this diverse target set allows CaM to take part in the regulation of several vital cell functions. To fully understand the structural basis of the regulation functions of CaM, the investigation of complexes of CaM and its targets is essential. In this minireview we give an outline of the different types of CaM - peptide complexes with 3D structure determined, also providing an overview of recently determined structures. We discuss factors defining the orientations of peptides within the complexes, as well as roles of anchoring residues. The emphasis is on complexes where multiple binding modes were found.

引用

页码：1102 / 1111

页数：10

共 78 条

[1] Structural basis for endothelial nitric oxide synthase binding to calmodulin [J].