Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites
Wang, DQ; Guo, M; Liang, Z; Fan, J; Zhu, ZQ; Zang, JY; Zhu, ZG; Li, XW; Teng, MK; Niu, LW; Dong, YH; Liu, P; Dong YH(董宇辉); 刘鹏(多)
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2005
卷号280期号:24页码:22962-22967
学科分类Biochemistry & Molecular Biology
DOI10.1074/jbc.M500464200
通讯作者Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China ; Univ Sci & Technol China, Chinese Acad Sci, Key Lab Struct Biol, Hefei 230026, Anhui, Peoples R China ; Univ Sci & Technol China, Sch Life Sci, Dept Mol & Cell Biol, Hefei 230026, Anhui, Peoples R China ; Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100039, Peoples R China
文章类型Article
英文摘要Vacuolar protein sorting protein 29 (Vps29p), which is involved in retrograde trafficking from prevacuolar endosomes to the trans-Golgi network, performs its biological functions by participating in the formation of a "retromer complex." In human cells, this complex comprises four conserved proteins: hVps35p, hVps29p, hVps26p, and sorting nexin 1 protein (SNX1). Here, we report the crystal structure of hVps29p at 2.1 angstrom resolution, the first three-dimensional structure of the retromer subunits. This novel structure adopts a four-layered alpha-beta-beta-alpha sandwich fold. hVps29p contains a metal-binding site that is very similar to the active sites of some proteins of the phosphodiesterase/nuclease protein family, indicating that hVps29p may carry out chemically similar functions. Structure and sequence conservation analysis suggests that hVps29p contains two protein-protein interaction sites. One site, which potentially serves as the interface between hVps29p and hVps35p, comprises 5 conserved hydrophobic and 8 hydrophilic residues. The other site is relatively more hydrophilic and may serve as a binding interface with hVps26p, SNX1, or other target proteins.
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
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语种英语
WOS记录号WOS:000229741800050
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被引频次:48[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/240204
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
作者单位中国科学院高能物理研究所
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Wang, DQ,Guo, M,Liang, Z,et al. Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2005,280(24):22962-22967.
APA Wang, DQ.,Guo, M.,Liang, Z.,Fan, J.,Zhu, ZQ.,...&刘鹏.(2005).Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites.JOURNAL OF BIOLOGICAL CHEMISTRY,280(24),22962-22967.
MLA Wang, DQ,et al."Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites".JOURNAL OF BIOLOGICAL CHEMISTRY 280.24(2005):22962-22967.
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