4XC5
CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1
Summary for 4XC5
| Entry DOI | 10.2210/pdb4xc5/pdb |
| Related | 1KKE 3EOY 3S6X 4GU3 4ODB |
| Descriptor | Outer capsid protein sigma-1, CHLORIDE ION, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | triple beta-spiral, beta-barrel, beta-spiral repeat, greek key motif, viral attachment protein, gm2 glycan alpha-2, 3-sialyllactose, junctional adhesion molecule a, viral capsid, viral protein |
| Biological source | Mammalian orthoreovirus 1 Lang (T1L) |
| Cellular location | Virion : P04506 |
| Total number of polymer chains | 3 |
| Total formula weight | 74940.76 |
| Authors | Reiss, K.,Stehle, T. (deposition date: 2014-12-17, release date: 2015-04-01, Last modification date: 2024-01-10) |
| Primary citation | Stettner, E.,Dietrich, M.H.,Reiss, K.,Dermody, T.S.,Stehle, T. Structure of Serotype 1 Reovirus Attachment Protein sigma 1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope. J.Virol., 89:6136-6140, 2015 Cited by PubMed Abstract: Mammalian orthoreoviruses use glycans and junctional adhesion molecule A (JAM-A) as attachment receptors. We determined the structure of serotype 1 reovirus attachment protein σ1 alone and in complex with JAM-A. Comparison with the structure of serotype 3 reovirus σ1 bound to JAM-A reveals that both σ1 proteins engage JAM-A with similar affinities and via conserved binding epitopes. Thus, σ1-JAM-A interactions are unlikely to explain the differences in pathogenesis displayed by these reovirus serotypes. PubMed: 25810543DOI: 10.1128/JVI.00433-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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