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Title: Tyrosine replacement of PSGL-1 reduces association kinetics with P- and L-selectin on the cell membrane
Author: Xiao BT(肖波涛); Tong CF(佟春芳); Jia XL(贾潇凌); Guo R(郭瑞); Lv SQ(吕守芹); Zhang Y(章燕); McEver RP; Zhu C; Long M(龙勉)
Source: BIOPHYSICAL JOURNAL
Issued Date: 2012-08-22
Volume: 103, Issue:4, Pages:777-785
Abstract: Binding of selectins to P-selectin glycoprotein ligand-1 (PSGL-1) mediates tethering and rolling of leukocytes on the endothelium during inflammation. Previous measurements obtained with a flow-chamber assay have shown that mutations of three tyrosines at the PSGL-1 N-terminus (Y46, Y48, and Y51) increase the reverse rates and their sensitivity to the force of bonds with P- and L-selectin. However, the effects of these mutations on the binding affinities and forward rates have not been studied. We quantified these effects by using an adhesion frequency assay to measure two-dimensional affinity and kinetic rates at zero force. Wild-type PSGL-1 has 2.2- to 8.5-fold higher binding affinities for P- and L-selectin than PSGL-1 mutants with two of three tyrosines substituted by phenylalanines, and 9.6- to 49-fold higher affinities than the PSGL-1 mutant with all three tyrosines replaced. In descending order, the affinity decreased from wild-type to Y48/51F, Y46/51F, Y46/48F, and Y46/48/51F. The affinity difference's were attributed to major changes in the forward rate and minor changes in the reverse rate, suggesting that these tyrosines regulate the accessibility of PSGL-1 to P- and L-selectin via electrostatic interactions, which is supported by molecular-dynamics simulations. Our results provide insights into the structure-function relationship of receptor-ligand binding at a single-residue level.
Keyword: Ligand Binding-Kinetics ; Glycoprotein Ligand-1 ; Molecular-Dynamics ; Adhesion ; Sulfation ; Proteins ; Glycosulfopeptides ; Identification ; Dissociation ; Recognition
Language: 英语
Indexed Type: SCI
Corresponding Author: Long, MA ; Chinese Acad Sci, Inst Mech, Key Lab Micrograv, Beijing 100080, Peoples R China.
Correspondent Email: cheng.zhu@bme.gatech.edu;mlong@imech.ac.cn
Related URLs: 查看原文
WOS ID: WOS:000307799100017
ISSN: 0006-3495
Rank: [Xiao, Botao;Tong, Chunfang; Jia, Xiaoling; Guo, Rui; Lu, Shouqin; Zhang, Yan; Long, Mian] Chinese Acad Sci, Inst Mech, Key Lab Micrograv, Beijing 100080, Peoples R China; [Xiao, Botao; Tong, Chunfang; Jia, Xiaoling; Guo, Rui; Lu, Shouqin; Zhang, Yan; Long, Mian] Chinese Acad Sci, Inst Mech, Ctr Biomech & Bioengn, Beijing 100080, Peoples R China; [Zhu, Cheng] Georgia Inst Technol, Coulter Dept Biomed Engn, Atlanta, GA 30332 USA; [McEver, Rodger P.] Oklahoma Med Res Fdn, Cardiovasc Biol Res Program, Oklahoma City, OK 73104 USA; [McEver, Rodger P.] Univ Oklahoma, Hlth Sci Ctr, Dept Biochem & Mol Biol, Oklahoma City, OK 73190 USA; [Xiao, Botao] Northwestern Univ, Dept Phys & Astron, Evanston, IL USA; [Xiao, Botao] Northwestern Univ, Dept Mol Biosci, Evanston, IL USA
Subject: 交叉与边缘领域的力学::生物力学
Department: NML分子-细胞生物力学与空间生命科学
Classification: 一类
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Content Type: 期刊论文
URI: http://dspace.imech.ac.cn/handle/311007/46605
Appears in Collections:国家微重力实验室_期刊论文

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肖波涛;佟春芳;贾潇凌;郭瑞;吕守芹;章燕;McEver RP;Zhu C;龙勉.Tyrosine replacement of PSGL-1 reduces association kinetics with P- and L-selectin on the cell membrane,BIOPHYSICAL JOURNAL,2012,103(4):777-785
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