Evidence map›Paper›PMID 26039348›Full record

ArticleStructure (London, England : 1993)2015

Computational Refinement and Validation Protocol for Proteins with Large Variable Regions Applied to Model HIV Env Spike in CD4 and 17b Bound State.

Muhibur Rasheed, Radhakrishna Bettadapura, Chandrajit Bajaj

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  12. Specific Substitutions in Region V2 of gp120Pathogens (Basel, Switzerland) · 2020
    Article
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  15. Review
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  18. Review
  19. Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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

3 authors at 1 institution in 1 country.

Muhibur RasheedComputer Science Department, The University of Texas at Austin, 1 University Station, Austin, TX 78712, USA.
Radhakrishna BettadapuraComputer Science Department, The University of Texas at Austin, 1 University Station, Austin, TX 78712, USA.
Chandrajit BajajComputer Science Department, The University of Texas at Austin, 1 University Station, Austin, TX 78712, USA. Electronic address: bajaj@cs.utexas.edu.
The University of Texas at Austin · US

Funding

Mathematical Chemical Imaging with Uncertainty Quantification R01GM117594 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BAJAJ, CHANDRAJIT L · 2015 to 2018
$1.6M
A New Approach to Rapid Protein-Protein DockingR01GM073087 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BAJAJ, CHANDRAJIT L · 2006 to 2008
$1.3M
Software Maintenance for Biomolecular ComplexesR01EB004873 · NIBIB · UNIVERSITY OF TEXAS AT AUSTIN · PI BAJAJ, CHANDRAJIT L · 2007 to 2010
$1.2M
Hierarchical Methods for Large BioMolecular ComplexesR01GM074258 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI BAJAJ, CHANDRAJIT L · 2005 to 2010
$778k
NIBIB NIH HHS R01 EB004873NIBIB NIH HHS R01-EB004873NIGMS NIH HHS R01 GM073087NIGMS NIH HHS R01-GM073087NIGMS NIH HHS R01 GM074258NIGMS NIH HHS R01-GM074258NIGMS NIH HHS R01 GM117594
6 · The paper itself

Abstract

Envelope glycoprotein gp120 of HIV-1 possesses several variable regions; their precise structure has been difficult to establish. We report a new model of gp120, in complex with antibodies CD4 and 17b, complete with its variable regions. The model was produced by a computational protocol that uses cryo-electron microscopy (EM) maps, atomic-resolution structures of the core, and information on binding interactions. Our model has excellent fit with EMD: 5020, is stereochemically and energetically favorable, and has the expected binding interfaces. Comparison of the ternary arrangement of the loops in this model with those bound to PGT122 and PGV04 suggested a possible motion of the V1V2 away from the CCR5 binding site and toward CD4. Our study also revealed that the CD4-bound state of the V1V2 loop is not optimal for gp120 bound with several neutralizing antibodies.

Indexed as

Models, MolecularAntibodies, NeutralizingCD4 AntigensCryoelectron MicroscopyHIV Envelope Protein gp120Protein BindingProtein ConformationAntibodies, NeutralizingCD4 AntigensHIV Envelope Protein gp120

Identifiers

PMID26039348
PMCPMC4474864
OpenAlexW1774721170

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.