Evidence map›Paper›PMID 20956299›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone.

Yang Mao, Xianzhong Xu, Wei Xu, Yuko Ishida, Walter S Leal, James B Ames, Jon Clardy

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 140 citations in OpenAlex.

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2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Yang MaoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Xianzhong Xu
Wei Xu
Yuko Ishida
Walter S Leal
James B Ames
Jon Clardy
University of California, Davis · USHarvard University · US

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023
$6.9M
STRUCTURAL STUDIES ON BIOACTIVE NATURAL PRODUCTSR01CA024487 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI CLARDY, JON · 1985 to 2009
$3.4M
Target-Based High-Throughput Screens for Plasmodium falciparum MalariaR21NS059404 · NINDS · HARVARD MEDICAL SCHOOL · PI CLARDY, JON · 2007 to 2010
$127k
NCI NIH HHS R01 CA024487NEI NIH HHS EY012347NEI NIH HHS R01 EY012347NINDS NIH HHS NS059404NINDS NIH HHS R21 NS059404
6 · The paper itself

Abstract

Culex mosquitoes introduce the pathogens responsible for filariasis, West Nile virus, St. Louis encephalitis, and other diseases into humans. Currently, traps baited with oviposition semiochemicals play an important role in detection efforts and could provide an environmentally friendly approach to controlling their populations. The odorant binding proteins (OBPs) in the female's antenna play a crucial, if yet imperfectly understood, role in sensing oviposition cues. Here, we report the X-ray crystallography and NMR 3D structures of OBP1 for Culex quinquefasciatus (CquiOBP1) bound to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP). In both studies, CquiOBP1 had the same overall six-helix structure seen in other insect OBPs, but a detailed analysis revealed an important previously undescribed feature. There are two models for OBP-mediated signal transduction: (i) direct release of the pheromone from an internal binding pocket in a pH-dependent fashion and (ii) detection of a pheromone-induced conformational change in the OBP·pheromone complex. Although CquiOBP1 binds MOP in a pH-dependent fashion, it lacks the C terminus required for the pH-dependent release model. This study shows that CquiOBP binds MOP in an unprecedented fashion using both a small central cavity for the lactone head group and a long hydrophobic channel for its tail.

Indexed as

Models, MolecularAnimalsCrystallography, X-RayCulexFemaleHydrogen-Ion ConcentrationInsect ProteinsOvipositionProtein BindingProtein Structure, TertiaryPyronesReceptors, OdorantSex AttractantsStructure-Activity Relationship6-acetoxy-5-hexadecanolideInsect Proteinsodorant-binding proteinPyronesReceptors, OdorantSex Attractants

Identifiers

PMID20956299
PMCPMC2973904
OpenAlexW2051213056

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.