Evidence map›Paper›PMID 27686537›Full record

ArticleBiochemistry2016

Thermodynamics of Nanobody Binding to Lactose Permease.

Parameswaran Hariharan, Magnus Andersson, Xiaoxu Jiang, Els Pardon, Jan Steyaert, H Ronald Kaback, Lan Guan

Abstract read
PubMed Full text at PMC Publisher
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. It takes two to tango: The dance of the permease.The Journal of general physiology · 2019
    Review
  3. Article
  4. Article
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 6 institutions in 3 countries.

Parameswaran HariharanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center , Lubbock, Texas 79430, United States.
Magnus AnderssonDepartment of Theoretical Physics and Swedish e-Science Research Center, Science for Life Laboratory, KTH Royal Institute of Technology , SE-171 21 Solna, Sweden.
Xiaoxu JiangDepartment of Physiology, University of California , Los Angeles, California 90095, United States.
Els PardonVIB Center for Structural Biology Research, VIB , 1050 Brussel, Belgium.
Jan SteyaertVIB Center for Structural Biology Research, VIB , 1050 Brussel, Belgium.
H Ronald KabackDepartment of Physiology, University of California , Los Angeles, California 90095, United States.
Lan GuanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center , Lubbock, Texas 79430, United States.
University of California, Los Angeles · USSwedish e-Science Research Centre · SETexas Tech University · USTexas Tech University Health Sciences Center · USVIB-VUB Center for Structural Biology · BEVrije Universiteit Brussel · BE

Funding

NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Novel capture reagents for membrane protein structure determinationR01GM095538 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2010 to 2013
$1.2M
NIDDK NIH HHS R01 DK051131NIGMS NIH HHS R01 GM095538
6 · The paper itself

Abstract

Camelid nanobodies (Nbs) raised against the outward-facing conformer of a double-Trp mutant of the lactose permease of Escherichia coli (LacY) stabilize the permease in outward-facing conformations. Isothermal titration calorimetry is applied herein to dissect the binding thermodynamics of two Nbs, one that markedly improves access to the sugar-binding site and another that dramatically increases the affinity for galactoside. The findings presented here show that both enthalpy and entropy contribute favorably to binding of the Nbs to wild-type (WT) LacY and that binding of Nb to double-Trp mutant G46W/G262W is driven by a greater enthalpy at an entropic penalty. Thermodynamic analyses support the interpretation that WT LacY is stabilized in outward-facing conformations like the double-Trp mutant with closure of the water-filled cytoplasmic cavity through conformational selection. The LacY conformational transition required for ligand binding is reflected by a favorable entropy increase. Molecular dynamics simulations further suggest that the entropy increase likely stems from release of immobilized water molecules primarily from the cytoplasmic cavity upon closure.

Indexed as

Single-Domain AntibodiesCalorimetryEscherichia coliMembrane Transport ProteinsMolecular Dynamics SimulationSubstrate SpecificityThermodynamicslactose permeaseMembrane Transport ProteinsSingle-Domain Antibodies

Identifiers

PMID27686537
PMCPMC6478161
OpenAlexW2525686239

What OpenQuestion holds

Textmetadata
LicenceTDM
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.