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4JHW

Crystal Structure of Respiratory Syncytial Virus Fusion Glycoprotein Stabilized in the Prefusion Conformation by Human Antibody D25

Summary for 4JHW
Entry DOI10.2210/pdb4jhw/pdb
Related4JHA
DescriptorD25 antigen-binding fragment heavy chain, D25 light chain, Fusion glycoprotein F0 (3 entities in total)
Functional Keywordsimmunoglobulin; type i fusion protein, membrane fusion, immune system
Biological sourceHomo sapiens
More
Cellular locationVirion membrane; Single-pass type I membrane protein: P03420
Total number of polymer chains3
Total formula weight102715.94
Authors
Primary citationMcLellan, J.S.,Chen, M.,Leung, S.,Graepel, K.W.,Du, X.,Yang, Y.,Zhou, T.,Baxa, U.,Yasuda, E.,Beaumont, T.,Kumar, A.,Modjarrad, K.,Zheng, Z.,Zhao, M.,Xia, N.,Kwong, P.D.,Graham, B.S.
Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody.
Science, 340:1113-1117, 2013
Cited by
PubMed Abstract: The prefusion state of respiratory syncytial virus (RSV) fusion (F) glycoprotein is the target of most RSV-neutralizing activity in human sera, but its metastability has hindered characterization. To overcome this obstacle, we identified prefusion-specific antibodies that were substantially more potent than the prophylactic antibody palivizumab. The cocrystal structure for one of these antibodies, D25, in complex with the F glycoprotein revealed D25 to lock F in its prefusion state by binding to a quaternary epitope at the trimer apex. Electron microscopy showed that two other antibodies, AM22 and 5C4, also bound to the newly identified site of vulnerability, which we named antigenic site Ø. These studies should enable design of improved vaccine antigens and define new targets for passive prevention of RSV-induced disease.
PubMed: 23618766
DOI: 10.1126/science.1234914
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

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數據於2024-11-06公開中

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