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气味结合蛋白:结构方面

Odorant-binding proteins: structural aspects.

作者信息

Pelosi P

机构信息

Istituto di Industrie Agrarie, University of Pisa, Italy.

出版信息

Ann N Y Acad Sci. 1998 Nov 30;855:281-93. doi: 10.1111/j.1749-6632.1998.tb10584.x.

Abstract

Structural data on odorant-binding proteins (OBPs), both in vertebrates and in insects, are reviewed and discussed. OBPs are soluble proteins interacting with odor molecules and pheromones in the perireceptor areas, the nasal mucus in vertebrates and the sensillar lymph in insects. The physiological function of these proteins is still uncertain, but information on their structure is abundant and accurate. Based on complete amino acid sequences, several subclasses have been identified, suggesting a role in odor discrimination. The OBPs of vertebrates belong to the family of lipocalins that includes proteins involved in the delivery of pheromonal messages. Those of insects do not bear significant similarity to any other class of proteins. The three-dimensional structure of the bovine OBP is a beta-barrel, while for insect OBPs a model has been proposed, mainly containing alpha-helix motifs. In some cases the amino acid residues involved in ligand binding have been identified with the use of photoaffinity label analogues.

摘要

本文综述并讨论了脊椎动物和昆虫中气味结合蛋白(OBP)的结构数据。OBP是一种可溶性蛋白,在感受器官区域与气味分子和信息素相互作用,在脊椎动物中存在于鼻黏液中,在昆虫中存在于感器淋巴液中。这些蛋白的生理功能仍不确定,但有关其结构的信息丰富且准确。基于完整的氨基酸序列,已鉴定出几个亚类,这表明其在气味辨别中发挥作用。脊椎动物的OBP属于脂质运载蛋白家族,该家族包括参与传递信息素信号的蛋白质。昆虫的OBP与其他任何一类蛋白质都没有显著的相似性。牛OBP的三维结构是一个β桶,而对于昆虫OBP,已提出了一个模型,主要包含α螺旋基序。在某些情况下,已使用光亲和标记类似物鉴定了参与配体结合的氨基酸残基。

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