当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > The mechanism underlying OBP heterodimer formation and the recognition of odors in Holotrichia oblita Faldermann.

The mechanism underlying OBP heterodimer formation and the recognition of odors in Holotrichia oblita Faldermann.

Abstract：

:Insect odorant-binding proteins (OBPs) play key roles in transport odors to receptors and contribute to insect survival. The cooperative interaction of HoblOBP1 and HoblOBP2 in Holotrichia oblita Faldermann (Coleoptera: Melolonthidae) could increase their binding capacity for ligands. In present study, molecular docking results showed that OBP1/OBP2 complex formed a large binding pocket and interacted with the ligands by hydrogen bonds and hydrophobic interactions. Then, nine amino acids for single site mutations, three paired for double sites, and negative control were mutated into alanine successfully by site-directed mutagenesis. Finally, fluorescence binding assays of these mutants showed that breaking one or two pairs of hydrogen bonds between HoblOBP1 and HoblOBP2 or formed with the ligands significantly decrease the binding affinity with the ligands. However, hydrophobic site mutants still showed slight binding affinity to the ligands. Therefore, the three pairs of hydrogen bonds involved in heterodimer formation and the five hydrogen bonding sites in binding pocket played a key role in response to odors in H. oblita. Our findings may promote further understanding of the mechanisms underlying OBP dimer formation and the role of OBP dimers in odor perception and discrimination.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Wei HS,Duan HX,Li KB,Zhang S,Wei ZJ,Yin J

doi

10.1016/j.ijbiomac.2019.10.182

subject

Has Abstract

pub_date

2020-06-01 00:00:00

pages

957-968

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)37055-2

journal_volume

152

pub_type

杂志文章

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