4.7 Review

PDZ domains and their binding partners: structure, specificity, and modification

期刊

CELL COMMUNICATION AND SIGNALING
卷 8, 期 -, 页码 -

出版社

BMC
DOI: 10.1186/1478-811X-8-8

关键词

-

资金

  1. National Cancer Institute [CA21765]
  2. National Institutes of Health, and the American Lebanese Syrian Associated Charities (ALSAC) [GM081492]

向作者/读者索取更多资源

PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction systems. This review discusses the structural characterization of PDZ domains and the use of recently emerging technologies such as proteomic arrays and peptide libraries to study the binding properties of PDZ-mediated interactions. Regulatory mechanisms responsible for PDZ-mediated interactions, such as phosphorylation in the PDZ ligands or PDZ domains, are also discussed. A better understanding of PDZ protein-protein interaction networks and regulatory mechanisms will improve our knowledge of many cellular and biological processes.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据