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- PDB-5awn: Crystal structure of Human anti-HIV-1 broadly neutralizing antibo... -

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Basic information

Entry
Database: PDB / ID: 5awn
TitleCrystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC176 Fab
Components
  • Heavy chain of 3BC176 Fab
  • Light chain of 3BC176 Fab
KeywordsIMMUNE SYSTEM / HIV-1 / Env / broadly neutralizing antibody
Function / homologyImmunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Function and homology information
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.887 Å
AuthorsLee, J.H. / Wilson, I.A. / Ward, A.B.
Funding support United States, 6items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)P01 AI082362 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)UM1 AI100663 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI084817 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI114401 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI098602 United States
Bill & Melinda Gates Foundation United States
CitationJournal: Nat Commun / Year: 2015
Title: Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.
Authors: Jeong Hyun Lee / Daniel P Leaman / Arthur S Kim / Alba Torrents de la Peña / Kwinten Sliepen / Anila Yasmeen / Ronald Derking / Alejandra Ramos / Steven W de Taeye / Gabriel Ozorowski / ...Authors: Jeong Hyun Lee / Daniel P Leaman / Arthur S Kim / Alba Torrents de la Peña / Kwinten Sliepen / Anila Yasmeen / Ronald Derking / Alejandra Ramos / Steven W de Taeye / Gabriel Ozorowski / Florian Klein / Dennis R Burton / Michel C Nussenzweig / Pascal Poignard / John P Moore / Per Johan Klasse / Rogier W Sanders / Michael B Zwick / Ian A Wilson / Andrew B Ward /
Abstract: The recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer. ...The recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer. By using biochemical, biophysical and computational methods, we map the previously unknown trimer epitopes of two related antibodies, 3BC315 and 3BC176. A cryo-EM reconstruction of a soluble Env trimer bound to 3BC315 Fab at 9.3 Å resolution reveals that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating trimer decay. In contrast, bnAb 35O22 binding to a partially overlapping quaternary epitope at the gp120-gp41 interface does not induce decay. A conserved gp41-proximal glycan at N88 was also shown to play a role in the binding kinetics of 3BC176 and 3BC315. Finally, our data suggest that the dynamic structure of the Env trimer influences exposure of bnAb epitopes.
History
DepositionJul 6, 2015Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 11, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Mar 23, 2022Group: Author supporting evidence / Database references / Category: database_2 / pdbx_audit_support
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization
Revision 1.3Nov 8, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.4Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
H: Heavy chain of 3BC176 Fab
L: Light chain of 3BC176 Fab


Theoretical massNumber of molelcules
Total (without water)48,1332
Polymers48,1332
Non-polymers00
Water5,513306
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3370 Å2
ΔGint-26 kcal/mol
Surface area19130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)41.732, 60.955, 87.239
Angle α, β, γ (deg.)90.00, 95.39, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Antibody Heavy chain of 3BC176 Fab


Mass: 24975.201 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
#2: Antibody Light chain of 3BC176 Fab


Mass: 23157.672 Da / Num. of mol.: 1 / Mutation: G108R, N112A, T114S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 306 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.3 Å3/Da / Density % sol: 46.45 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 0.1 M sodium citrate pH 5.6, 20% 2-propanol, 20% PEG 4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1 Å
DetectorType: NOIR-1 / Detector: CCD / Date: Oct 18, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.887→50 Å / Num. obs: 35026 / % possible obs: 99.7 % / Redundancy: 3.7 % / Net I/σ(I): 16.7

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
PHASERphasing
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5CCK

5cck


Resolution: 1.887→49.894 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 22.73 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.223 2000 5.71 %
Rwork0.1771 --
obs0.1797 35026 99.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.887→49.894 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3270 0 0 306 3576
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0073383
X-RAY DIFFRACTIONf_angle_d1.1484607
X-RAY DIFFRACTIONf_dihedral_angle_d12.6191210
X-RAY DIFFRACTIONf_chiral_restr0.046515
X-RAY DIFFRACTIONf_plane_restr0.006591
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8869-1.93410.27851360.24412227X-RAY DIFFRACTION95
1.9341-1.98640.29081430.20592378X-RAY DIFFRACTION99
1.9864-2.04490.24431400.18882321X-RAY DIFFRACTION99
2.0449-2.11090.26011440.19622361X-RAY DIFFRACTION99
2.1109-2.18630.231410.18112334X-RAY DIFFRACTION100
2.1863-2.27390.26521430.20112344X-RAY DIFFRACTION99
2.2739-2.37740.26181420.19122352X-RAY DIFFRACTION100
2.3774-2.50270.2571430.19852374X-RAY DIFFRACTION100
2.5027-2.65950.25831440.22375X-RAY DIFFRACTION100
2.6595-2.86480.25021420.20622360X-RAY DIFFRACTION100
2.8648-3.15310.25391440.19552370X-RAY DIFFRACTION100
3.1531-3.60920.21831440.16592380X-RAY DIFFRACTION100
3.6092-4.54670.16841460.13612403X-RAY DIFFRACTION100
4.5467-49.91120.15191480.14432447X-RAY DIFFRACTION100

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