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3d0g
From Proteopedia
| 3d0g, resolution 2.80Å () | |||||||||
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| Sites: | , , , , , , , and | ||||||||
| Ligands: | , , , | ||||||||
| Gene: | ACE2 (Paguma larvata, Homo sapiens), S (Human SARS coronavirus) | ||||||||
| Related: | 2ajf, 3d0h, 3d0i
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2
It is believed that a novel coronavirus, severe acute respiratory syndrome coronavirus (SARS-CoV), was passed from palm civets to humans and caused the epidemic of SARS in 2002 to 2003. The major species barriers between humans and civets for SARS-CoV infections are the specific interactions between a defined receptor-binding domain (RBD) on a viral spike protein and its host receptor, angiotensin-converting enzyme 2 (ACE2). In this study a chimeric ACE2 bearing the critical N-terminal helix from civet and the remaining peptidase domain from human was constructed, and it was shown that this construct has the same receptor activity as civet ACE2. In addition, crystal structures of the chimeric ACE2 complexed with RBDs from various human and civet SARS-CoV strains were determined. These structures, combined with a previously determined structure of human ACE2 complexed with the RBD from a human SARS-CoV strain, have revealed a structural basis for understanding the major species barriers between humans and civets for SARS-CoV infections. They show that the major species barriers are determined by interactions between four ACE2 residues (residues 31, 35, 38, and 353) and two RBD residues (residues 479 and 487), that early civet SARS-CoV isolates were prevented from infecting human cells due to imbalanced salt bridges at the hydrophobic virus/receptor interface, and that SARS-CoV has evolved to gain sustained infectivity for human cells by eliminating unfavorable free charges at the interface through stepwise mutations at positions 479 and 487. These results enhance our understanding of host adaptations and cross-species infections of SARS-CoV and other emerging animal viruses.
Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections., Li F, J Virol. 2008 Jul;82(14):6984-91. Epub 2008 Apr 30. PMID:18448527
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3D0G is a 4 chains structure of sequences from Human sars coronavirus and Paguma larvata, homo sapiens. Full crystallographic information is available from OCA.
Reference
- Li F. Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections. J Virol. 2008 Jul;82(14):6984-91. Epub 2008 Apr 30. PMID:18448527
Page seeded by OCA on Tue Feb 17 15:12:13 2009
Categories: Human sars coronavirus | Paguma larvata, homo sapiens | Li, F. | Ace2 | Alternative splicing | Angiotensin-converting enzyme 2 | Carboxypeptidase | Chloride | Coiled coil | Cross-species infection | Envelope protein | Glycoprotein | Host adaptation | Host-virus interaction | Human | Hydrolase | Lipoprotein | Membrane | Metal-binding | Metalloprotease | Palm civet | Palmitate | Polymorphism | Protease | Rbd | Receptor-binding domain | Sars coronavirus | Secreted | Spike protein | Transmembrane | Virion | Virulence | Virus-host interface | Zinc
