Evidence map›Paper›PMID 27324153›Full record

ArticleBiochemistry2016

Elucidation of Lipid Binding Sites on Lung Surfactant Protein A Using X-ray Crystallography, Mutagenesis, and Molecular Dynamics Simulations.

Boon Chong Goh, Huixing Wu, Michael J Rynkiewicz, Klaus Schulten, Barbara A Seaton, Francis X McCormack

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Linking Lipid Metabolism and Immune Function: New Insights into Chronic Respiratory Diseases.Pathophysiology : the official journal of the International Society for Pathophysiology · 2025
    Review
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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

6 authors at 3 institutions in 1 country.

Boon Chong GohBeckman Institute and Department of Physics, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Huixing WuDivision of Pulmonary, Critical Care and Sleep Medicine, Department of Internal Medicine, The University of Cincinnati , Cincinnati, Ohio 45267, United States.
Michael J RynkiewiczDepartment of Physiology and Biophysics, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Klaus SchultenBeckman Institute and Department of Physics, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Barbara A SeatonDepartment of Physiology and Biophysics, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Francis X McCormackDivision of Pulmonary, Critical Care and Sleep Medicine, Department of Internal Medicine, The University of Cincinnati , Cincinnati, Ohio 45267, United States.
Boston University · USUniversity of Cincinnati · USUniversity of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SCHULTEN, KLAUS · 2012 to 2021
$19.0M
Collectins and Innate Defense against Inhaled PathogensP01AI083222 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SEATON, BARBARA A · 2009 to 2010
$4.9M
NIAID NIH HHS P01 AI083222NIGMS NIH HHS P41 GM104601
6 · The paper itself

Abstract

Surfactant protein A (SP-A) is a collagenous C-type lectin (collectin) that is critical for pulmonary defense against inhaled microorganisms. Bifunctional avidity of SP-A for pathogen-associated molecular patterns (PAMPs) such as lipid A and for dipalmitoylphosphatidylcholine (DPPC), the major component of surfactant membranes lining the air-liquid interface of the lung, ensures that the protein is poised for first-line interactions with inhaled pathogens. To improve our understanding of the motifs that are required for interactions with microbes and surfactant structures, we explored the role of the tyrosine-rich binding surface on the carbohydrate recognition domain of SP-A in the interaction with DPPC and lipid A using crystallography, site-directed mutagenesis, and molecular dynamics simulations. Critical binding features for DPPC binding include a three-walled tyrosine cage that binds the choline headgroup through cation-π interactions and a positively charged cluster that binds the phosphoryl group. This basic cluster is also critical for binding of lipid A, a bacterial PAMP and target for SP-A. Molecular dynamics simulations further predict that SP-A binds lipid A more tightly than DPPC. These results suggest that the differential binding properties of SP-A favor transfer of the protein from surfactant DPPC to pathogen membranes containing appropriate lipid PAMPs to effect key host defense functions.

Indexed as

1,2-DipalmitoylphosphatidylcholineAnimalsBinding SitesCrystallography, X-RayMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationProtein ConformationProteolipidsPulmonary Surfactant-Associated Protein APulmonary SurfactantsRats1,2-DipalmitoylphosphatidylcholineProteolipidsPulmonary Surfactant-Associated Protein APulmonary Surfactants

Identifiers

PMID27324153
PMCPMC5663190
OpenAlexW2464948671

What OpenQuestion holds

Textmetadata
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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.