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Yorodumi- EMDB-21372: Cryo-EM structure of stabilized HIV-1 Env trimer CAP256.wk34.c80 ... -
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Basic information
| Entry | Database: EMDB / ID: EMD-21372 | |||||||||
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| Title | Cryo-EM structure of stabilized HIV-1 Env trimer CAP256.wk34.c80 SOSIP.RnS2 | |||||||||
 Map data | Sharpened map | |||||||||
 Sample | 
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 Keywords | V1V2 / VRC26 / CAP256 / HIV-1 / SOSIP / Vaccine / Superinfecting / IMMUNE SYSTEM | |||||||||
| Function / homology |  Function and homology informationpositive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane ...positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / membrane Similarity search - Function  | |||||||||
| Biological species | ![]()  Human immunodeficiency virus 1 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.71 Å | |||||||||
 Authors | Gorman J / Kwong PD | |||||||||
| Funding support |   United States, 1 items 
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 Citation |  Journal: Cell Rep / Year: 2020Title: Structure of Super-Potent Antibody CAP256-VRC26.25 in Complex with HIV-1 Envelope Reveals a Combined Mode of Trimer-Apex Recognition. Authors: Jason Gorman / Gwo-Yu Chuang / Yen-Ting Lai / Chen-Hsiang Shen / Jeffrey C Boyington / Aliaksandr Druz / Hui Geng / Mark K Louder / Krisha McKee / Reda Rawi / Raffaello Verardi / Yongping ...Authors: Jason Gorman / Gwo-Yu Chuang / Yen-Ting Lai / Chen-Hsiang Shen / Jeffrey C Boyington / Aliaksandr Druz / Hui Geng / Mark K Louder / Krisha McKee / Reda Rawi / Raffaello Verardi / Yongping Yang / Baoshan Zhang / Nicole A Doria-Rose / Bob Lin / Penny L Moore / Lynn Morris / Lawrence Shapiro / John R Mascola / Peter D Kwong /   ![]() Abstract: Antibodies targeting the V1V2 apex of the HIV-1 envelope (Env) trimer comprise one of the most commonly elicited categories of broadly neutralizing antibodies. Structures of these antibodies indicate ...Antibodies targeting the V1V2 apex of the HIV-1 envelope (Env) trimer comprise one of the most commonly elicited categories of broadly neutralizing antibodies. Structures of these antibodies indicate diverse modes of Env recognition typified by antibodies of the PG9 class and the PGT145 class. The mode of recognition, however, has been unclear for the most potent of the V1V2 apex-targeting antibodies, CAP256-VRC26.25 (named for donor-lineage.clone and referred to hereafter as VRC26.25). Here, we determine the cryoelectron microscopy structure at 3.7 Å resolution of the antigen-binding fragment of VRC26.25 in complex with the Env trimer thought to have initiated the lineage. The 36-residue protruding loop of VRC26.25 displays recognition incorporating both strand-C interactions similar to the PG9 class and V1V2 apex insertion similar to the PGT145 class. Structural elements of separate antibody classes can thus intermingle to form a "combined" class, which in this case yields an antibody of extraordinary potency.  | |||||||||
| History | 
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Structure visualization
| Movie | 
 
 
  Movie viewer | 
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| Structure viewer | EM map:  SurfView Molmil Jmol/JSmol | 
| Supplemental images | 
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Downloads & links
-EMDB archive
| Map data |  emd_21372.map.gz | 117 MB |  EMDB map data format | |
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| Header (meta data) |  emd-21372-v30.xml emd-21372.xml | 20.4 KB 20.4 KB  | Display Display  |  EMDB header | 
| Images |  emd_21372.png | 119.8 KB | ||
| Masks |  emd_21372_msk_1.map | 125 MB |  Mask map | |
| Filedesc metadata |  emd-21372.cif.gz | 6.7 KB | ||
| Others |  emd_21372_additional.map.gz emd_21372_half_map_1.map.gz emd_21372_half_map_2.map.gz | 30.3 MB 116.1 MB 116.1 MB  | ||
| Archive directory |  http://ftp.pdbj.org/pub/emdb/structures/EMD-21372 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21372 | HTTPS FTP  | 
-Validation report
| Summary document |  emd_21372_validation.pdf.gz | 1004.4 KB | Display |  EMDB validaton report | 
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| Full document |  emd_21372_full_validation.pdf.gz | 1004 KB | Display | |
| Data in XML |  emd_21372_validation.xml.gz | 14 KB | Display | |
| Data in CIF |  emd_21372_validation.cif.gz | 16.5 KB | Display | |
| Arichive directory |  https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21372 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21372 | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 6vrwMC ![]() 6vttC M: atomic model generated by this map C: citing same article (  | 
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| Similar structure data | 
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Links
| EMDB pages |  EMDB (EBI/PDBe) /  EMDataResource | 
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| Related items in Molecule of the Month | 
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Map
| File |  Download / File: emd_21372.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Sharpened map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
 
 Images are generated by Spider.  | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.061 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density | 
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML: 
 CCP4 map header: 
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-Supplemental data
-Mask #1
| File |  emd_21372_msk_1.map | ||||||||||||
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| Density Histograms | 
-Additional map: Unnsharpened map
| File | emd_21372_additional.map | ||||||||||||
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| Annotation | Unnsharpened map | ||||||||||||
| Projections & Slices | 
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| Density Histograms | 
-Half map: Half map A
| File | emd_21372_half_map_1.map | ||||||||||||
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| Annotation | Half map A | ||||||||||||
| Projections & Slices | 
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| Density Histograms | 
-Half map: Half map B
| File | emd_21372_half_map_2.map | ||||||||||||
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| Annotation | Half map B | ||||||||||||
| Projections & Slices | 
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| Density Histograms | 
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Sample components
-Entire : HIV-1 Env trimer CAP256 SU.wk34.80 SOSIP.RnS2
| Entire | Name: HIV-1 Env trimer CAP256 SU.wk34.80 SOSIP.RnS2 | 
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| Components | 
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-Supramolecule #1: HIV-1 Env trimer CAP256 SU.wk34.80 SOSIP.RnS2
| Supramolecule | Name: HIV-1 Env trimer CAP256 SU.wk34.80 SOSIP.RnS2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 | 
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| Source (natural) | Organism: ![]()  Human immunodeficiency virus 1 | 
-Macromolecule #1: Envelope glycoprotein gp120
| Macromolecule | Name: Envelope glycoprotein gp120 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO | 
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| Source (natural) | Organism: ![]()  Human immunodeficiency virus 1 | 
| Molecular weight | Theoretical: 53.322434 KDa | 
| Recombinant expression | Organism:  Homo sapiens (human) | 
| Sequence | String: GLWVTVYYGV PVWREAKTTL FCASDAKSYE KEVHNVWATH ACVPTDPNPQ ELVLENVTEN FNMWKNDMVD QMHEDIISLW  DQSLKPCVK LTPLCVTLNC SDAKVNATYK GTREEIKNCS FNATTELRDK KRREYALFYR LDIVPLSGEG NNNSEYRLIN C NTSVITQI  ...String:  GLWVTVYYGV PVWREAKTTL FCASDAKSYE KEVHNVWATH ACVPTDPNPQ ELVLENVTEN FNMWKNDMVD QMHEDIISLW  DQSLKPCVK LTPLCVTLNC SDAKVNATYK GTREEIKNCS FNATTELRDK KRREYALFYR LDIVPLSGEG NNNSEYRLIN C NTSVITQI CPKVTFDPIP IHYCAPAGYA ILKCNNKTFN GTGPCNNVST VQCTHGIKPV VSTQLLLNGS LAEEEIIIRS EN LTDNVKT IIVHLNESVE ITCTRPNNMT RKSVRIGPGQ TFYALGDIIG DIRQPHCNIS EIKWEKTLQR VSEKLREHFN KTI IFNQSS GGDLEITTHS FNCGGEFFYC NTSDLFFNKT FNETYSTGSN STNSTITLPC RIKQIINMWQ EVGRAMYAPP IAGN ITCKS NITGLLLTRD GGGNNSTKET FRPGGGNMRD NWRSELYKYK VVEVKPLGIA PTECNRTVVQ RRRRRR  | 
-Macromolecule #2: Envelope glycoprotein gp41
| Macromolecule | Name: Envelope glycoprotein gp41 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO | 
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| Source (natural) | Organism: ![]()  Human immunodeficiency virus 1 | 
| Molecular weight | Theoretical: 17.355703 KDa | 
| Recombinant expression | Organism:  Homo sapiens (human) | 
| Sequence | String:  AVVGLGAVFL GFLGAAGSTM GAASNTLTVQ ARQLLSGIVQ QQSNLLRAPE AQQHMLQLGV WGFKQLQARV LAIERYLEVQ  QLLGMWGCS GKLICCTNVP WNSSWSNKTY NEIWDNMTWM QWDREIGNYT DTIYKLLEVS QFQQEINEKD NLTLD  | 
-Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 39 / Formula: NAG | 
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| Molecular weight | Theoretical: 221.208 Da | 
| Chemical component information | ![]() ChemComp-NAG:   | 
-Experimental details
-Structure determination
| Method | cryo EM | 
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 Processing | single particle reconstruction | 
| Aggregation state | particle | 
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Sample preparation
| Concentration | 2 mg/mL | 
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| Buffer | pH: 7.4 / Component - Formula: PBS | 
| Grid | Model: C-flat-1.2/1.3 4C / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY | 
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV | 
| Details | CAP256 SU.wk34.80 SOSIP.RnS2 | 
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Electron microscopy
| Microscope | FEI TITAN KRIOS | 
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 1760 / Average exposure time: 10.0 sec. / Average electron dose: 74.41 e/Å2 | 
| Electron beam | Acceleration voltage: 300 kV / Electron source:  FIELD EMISSION GUN | 
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD | 
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN | 
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company  | 
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About Yorodumi


Keywords
Human immunodeficiency virus 1
Authors
United States, 1 items 
Citation
UCSF Chimera













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Homo sapiens (human)
Processing

