[English] 日本語
![](img/lk-miru.gif)
- PDB-6vsj: Cryo-electron microscopy structure of mouse coronavirus spike pro... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6vsj | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-electron microscopy structure of mouse coronavirus spike protein complexed with its murine receptor | ||||||
![]() |
| ||||||
![]() | VIRAL PROTEIN / MHV spike / CEACAM1a / Complex / Glycoprotein | ||||||
Function / homology | ![]() Fibronectin matrix formation / granulocyte colony-stimulating factor receptor binding / positive regulation of homophilic cell adhesion / Post-translational modification: synthesis of GPI-anchored proteins / regulation of endothelial cell differentiation / insulin receptor internalization / negative regulation of cytotoxic T cell degranulation / granulocyte colony-stimulating factor signaling pathway / regulation of homophilic cell adhesion / regulation of sprouting angiogenesis ...Fibronectin matrix formation / granulocyte colony-stimulating factor receptor binding / positive regulation of homophilic cell adhesion / Post-translational modification: synthesis of GPI-anchored proteins / regulation of endothelial cell differentiation / insulin receptor internalization / negative regulation of cytotoxic T cell degranulation / granulocyte colony-stimulating factor signaling pathway / regulation of homophilic cell adhesion / regulation of sprouting angiogenesis / regulation of epidermal growth factor receptor signaling pathway / regulation of blood vessel remodeling / negative regulation of hepatocyte proliferation / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of lipid biosynthetic process / bile acid transmembrane transporter activity / negative regulation of T cell mediated cytotoxicity / regulation of endothelial cell migration / negative regulation of granulocyte differentiation / insulin catabolic process / Cell surface interactions at the vascular wall / common myeloid progenitor cell proliferation / Toll-like receptor binding / negative regulation of interleukin-1 production / negative regulation of fatty acid biosynthetic process / positive regulation of vasculogenesis / cell-cell adhesion via plasma-membrane adhesion molecules / regulation of immune system process / negative regulation of platelet aggregation / cell-cell junction organization / bile acid and bile salt transport / negative regulation of vascular permeability / negative regulation of bone resorption / wound healing, spreading of cells / ciliary membrane / negative regulation of cytokine production / microvillus membrane / negative regulation of T cell receptor signaling pathway / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / blood vessel development / negative regulation of osteoclast differentiation / lateral plasma membrane / negative regulation of T cell proliferation / transport vesicle / Neutrophil degranulation / regulation of ERK1 and ERK2 cascade / protein tyrosine kinase binding / basal plasma membrane / regulation of cell growth / adherens junction / negative regulation of protein kinase activity / endocytosis involved in viral entry into host cell / cellular response to insulin stimulus / cell-cell junction / cell junction / virus receptor activity / host cell Golgi apparatus / membrane => GO:0016020 / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / protein dimerization activity / calmodulin binding / cell adhesion / apical plasma membrane / external side of plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / protein kinase binding / host cell plasma membrane / virion membrane / cell surface / signal transduction / protein homodimerization activity / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.94 Å | ||||||
![]() | Shang, J. / Wan, Y.S. / Liu, C. / Yount, B. / Gully, K. / Yang, Y. / Auerbach, A. / Peng, G.Q. / Baric, R. / Li, F. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry. Authors: Jian Shang / Yushun Wan / Chang Liu / Boyd Yount / Kendra Gully / Yang Yang / Ashley Auerbach / Guiqing Peng / Ralph Baric / Fang Li / ![]() ![]() Abstract: Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse ...Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses. | ||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | Molecule: ![]() ![]() |
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 646.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 523.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 21377MC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
#1: Protein | Mass: 141118.797 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 23678.691 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Sugar | ChemComp-NAG / Has ligand of interest | N | |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Source (natural) |
| ||||||||||||||||||||||||
Source (recombinant) |
| ||||||||||||||||||||||||
Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
Buffer component |
| ||||||||||||||||||||||||
Specimen | Conc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 77 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-
Processing
CTF correction | Type: NONE |
---|---|
Symmetry | Point symmetry: C3 (3 fold cyclic) |
3D reconstruction | Resolution: 3.94 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 82923 / Symmetry type: POINT |