Pattern and Temporal Sequence of Sulfation of CCR5 N-Terminal Peptides by Tyrosylprotein Sulfotransferase-2: An Assessment of the Effects of N-Terminal Residues
Pattern and Temporal Sequence of Sulfation of CCR5 N-Terminal Peptides by Tyrosylprotein Sulfotransferase-2: An Assessment of the Effects of N-Terminal Residues
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DOI：
10.1021/bi900285c
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发表时间：
2009-06-16
期刊：
影响因子：
2.9
通讯作者：
Leary, Julie A.
中科院分区：
文献类型：
--
作者：
Jen, Connie H.;Moore, Kevin L.;Leary, Julie A.
CC趋化因子受体5 （CCR5）是几种炎症趋化因子的受体，也是HIV-1的辅助受体。趋化因子受体n端区域酪氨酸的翻译后硫酸化已被证明在趋化因子配体的结合亲和力中是重要的。此外，CCR5的硫酸化对于介导与HIV-1包膜蛋白gp120的相互作用至关重要。通过酪氨酸蛋白硫转移酶-2 （tyrosylprotein sulfotransferase -2, TPST-2）体外酶促磺化、RP-HPLC分离产物和质谱分析，确定了CCR5和CCR8 n端肽的主要磺化途径和肽的变化。结果表明，CCR5和CCR8的磺化模式和磺化速率与tyr3的n端氨基酸数目有关。本文的结果解决了先前看似矛盾的研究，并描述了n端趋化因子受体肽的时间磺化。
CC chemokine receptor 5 (CCR5) is the receptor for several inflammatory chemokines and is a coreceptor for HIV-1. Posttranslational sulfation of tyrosines in the N-terminal regions of chemokine receptors has been shown to be important in the binding affinity for chemokine ligands. In addition, sulfation of CCR5 is crucial for mediating interactions with HIV-1 envelope protein gp120. The major sulfation pathway for peptides derived from the N-terminal domains of CCR5 and CCR8 and variations of the peptides were determined by in vitro enzymatic sulfation by tyrosylprotein sulfotranferase-2 (TPST-2), subsequent separation of products by RP-HPLC, and mass spectrometry analysis. It was found that the patterns of sulfation and the rates of sulfation for CCR5 and CCR8 depend on the number of amino acids N-terminal of Tyr-3. Results herein address previous seemingly contradictory studies and delineate the temporal sulfation of N-terminal chemokine receptor peptides.