Olfactory marker protein (OMP) exhibits a β-clam fold in solution:: Implications for target peptide interaction and olfactory signal transduction
Olfactory marker protein (OMP) exhibits a β-clam fold in solution:: Implications for target peptide interaction and olfactory signal transduction
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DOI：
10.1016/s0022-2836(02)00282-6
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发表时间：
2002-06-07
影响因子：
5.6
通讯作者：
Margolis, F
中科院分区：
文献类型：
--
作者：
Baldisseri, DM;Margolis, JW;Margolis, F
嗅觉标记蛋白（Olfactory marker protein，OMP）是一种普遍存在于脊椎动物成熟嗅觉感受神经元中的细胞质蛋白。电生理和行为学研究表明，它是嗅觉信号转导通路的调节剂。在这里，我们证明了OMP的溶液结构，如通过NMR研究所确定的，是由八条β链组成的单一球状结构域蛋白，形成彼此正交取向的两个β折叠，因此表现出“β-蛤”或“β-三明治”折叠：β-折叠1由β 3-β 8-β 1-β 2组成，β-折叠2包含β 6-β 5-β 4-β 7。插入包括位于β-clam相对侧的两个长α-螺旋和三个柔性环。β-链β 6-β 5-β 4-β 7-β 2-β 1-β 8-β 3的并置形成连续弯曲的表面并包围β-蛤的一侧。由两个β折叠形成的“裂缝”与β折叠的封闭端相对。使用肽滴定系列，我们已经确定了这个裂缝作为Bex 1蛋白衍生的肽的结合表面。在OMP中发现的Bex 1肽结合表面附近的高度保守的Omega环结构可能是与其在调节嗅觉信号转导中的作用相关的额外的OMP-蛋白质相互作用的位点。因此，OMP和Bex 1蛋白之间的相互作用可以促进OMP和嗅觉信号通路的其他组分之间的相互作用。(C)2002爱思唯尔科技有限公司。保留所有权利。
Olfactory marker protein (OMP) is a ubiquitous, cytoplasmic protein found in mature olfactory receptor neurons of all vertebrates. Electrophysiological and behavioral studies demonstrate that it is a modulator of the olfactory signal transduction pathway. Here, we demonstrate that the solution structure of OMP, as determined by NMR studies, is a single globular domain protein comprised of eight beta-strands forming two beta-sheets oriented orthogonally to one another, thus exhibiting a "beta-clam" or "beta-sandwich" fold: beta-sheet 1 is comprised of beta3-beta8-beta1-beta2 and beta-sheet 2 contains beta6-beta5-beta4-beta7. Insertions include two, long alpha-helices located on opposite sides of the beta-clam and three flexible loops. The juxtaposition of beta-strands beta6-beta5-beta4-beta7-beta2-beta1-beta8-beta3 forms a continuously curved surface and encloses one side of the beta-clam. The "cleft" formed by the two beta-sheets is opposite to the closed end of the beta-clam. Using a peptide titration series, we have identified this cleft as the binding surface for a peptide derived from the Bex1 protein. The highly conserved Omega-loop structure adjacent to the Bex1 peptide-binding surface found in OMP may be the site of additional OMP-protein interactions related to its role in modulating olfactory signal transduction. Thus, the interaction between the OMP and Bex1 proteins could facilitate the interaction between OMP and other components of the olfactory signaling pathway. (C) 2002 Elsevier Science Ltd. All rights reserved.