2AJF
Structure of SARS coronavirus spike receptor-binding domain complexed with its receptor
Summary for 2AJF
| Entry DOI | 10.2210/pdb2ajf/pdb |
| Descriptor | Angiotensin-converting enzyme-Related Carboxypeptidase (Ace2), SARS-coronavirus spike protein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | antiparallel beta sheet, extended loop, hydrolase-viral protein complex, hydrolase/viral protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 182055.53 |
| Authors | Li, F.,Li, W.,Farzan, M.,Harrison, S.C. (deposition date: 2005-08-01, release date: 2005-09-20, Last modification date: 2024-12-25) |
| Primary citation | Li, F.,Li, W.,Farzan, M.,Harrison, S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science, 309:1864-1868, 2005 Cited by PubMed Abstract: The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines. PubMed: 16166518DOI: 10.1126/science.1116480 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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