Common mechanism of ligand recognition by group II/III WW domains - Redefining their functional classification
Common mechanism of ligand recognition by group II/III WW domains - Redefining their functional classification
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DOI：
10.1074/jbc.m404719200
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发表时间：
2004-07-23
影响因子：
4.8
通讯作者：
Tanokura, M
中科院分区：
文献类型：
--
作者：
Kato, Y;Nagata, K;Tanokura, M
WW结构域是一个众所周知的蛋白质模块，其通过结合含脯氨酸的配体介导蛋白质与蛋白质的相互作用。基于配体偏好，WW结构域已被分为四个主要组。据报道，II和III组WW结构域分别结合脯氨酸-亮氨酸和脯氨酸-精氨酸基序。在本研究中，使用表面等离子体共振技术，我们已经表明，这些WW域具有几乎无法区分的配体偏好和动力学性质。因此，我们建议将第II组和第III组WW域合并为一个组（第II/III组）。与I组和IV组WW结构域不同，II/III组WW结构域可以结合简单的聚脯氨酸以及脯氨酸-亮氨酸和脯氨酸-精氨酸基序，并且它们具有类似于SH 3结构域的两个Xaa-脯氨酸（其中Xaa是任何氨基酸）结合槽。我们的工作分配组II和III WW域的一个更大的家庭的聚脯氨酸结合模块和蛋白质，其中包括SH 3域和profilin。由于聚脯氨酸属于最常见的肽基序在几个基因组中，我们的研究意味着通用的重要性组II/III WW域的信号。
WW domain is a well known protein module that mediates protein to protein interactions by binding to proline-containing ligands. Based on the ligand predilections, the WW domains have been classified into four major groups. Group II and III WW domains have been reported to bind the proline-leucine and proline-arginine motifs, respectively. In the present study, using surface plasmon resonance technique we have shown that these WW domains have almost indistinguishable ligand preferences and kinetic properties. Hence, we propose that Group II and III WW domains should be joined together as one group ( Group II/III). Unlike Group I and IV WW domains, Group II/III WW domains can bind simple polyprolines as well as the proline-leucine and proline-arginine motifs, and they possess two Xaa-proline (where Xaa is any amino acid) binding grooves similar to SH3 domains. Our work assigns Group II and III WW domains to a larger family of polyproline-binding modules and proteins, which includes SH3 domains and profilin. Because polyprolines belong to the most frequently found peptide motifs in several genomes, our study implies the versatile importance of Group II/III WW domains in signaling.