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Structural insights into phospholipase D function

delete2021-01-01
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OA
AI
Y
Yuanfa Yao
J
Jianxu Li
Y
Yinyan Lin
J
Jiaqiang Zhou
张鹏 cover
张鹏 (Peng Zhang) *
许迎科 (Yingke Xu) *
DOI:10.1016/j.plipres.2020.101070delete
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Abstract

Abstract

En 中文
Phospholipase D (PLD) and its metabolic active product phosphatidic acid (PA) engage in a wide range of physiopathologic processes in the cell. PLDs have been considered as a potential and promising drug target. Recently, the crystal structures of PLDs in mammalian and plant have been solved at atomic resolution. These achievements allow us to understand the structural differences among different species of PLDs and the functions of their key domains. In this review, we summarize the sequence and structure of different species of PLD isoforms, and discuss the structural mechanisms for PLD interactions with their binding partners and the functions of each key domain in the regulation of PLDs activation and catalytic reaction.
Keywords:
Phospholipase D
Phosphatidic acid
Crystal structure
HKD domain
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Journal

Progress in Lipid Research cover
Progress in Lipid Research
IF:
14.9
Papers:
703
Citations:
8.0K

Organization

C
center for excellence in molecular plant sciences, cas
Scholars:
883
Papers: 599
Citations: 0
C
chinese academy of sciences
Scholars:
56.5W
Papers: 44.9W
Citations: 704
Z
zhejiang university
Scholars:
17.6W
Papers: 12.1W
Citations: 152
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