1VLK
STRUCTURE OF VIRAL INTERLEUKIN-10
Summary for 1VLK
| Entry DOI | 10.2210/pdb1vlk/pdb |
| Descriptor | VIRAL INTERLEUKIN-10 (2 entities in total) |
| Functional Keywords | cytokine, glycoprotein |
| Biological source | Human herpesvirus 4 (Epstein-Barr virus) |
| Cellular location | Secreted (Potential): P03180 |
| Total number of polymer chains | 1 |
| Total formula weight | 17162.71 |
| Authors | Zdanov, A.,Schalk-Hihi, C.,Wlodawer, A. (deposition date: 1997-02-14, release date: 1997-04-01, Last modification date: 2024-10-23) |
| Primary citation | Zdanov, A.,Schalk-Hihi, C.,Menon, S.,Moore, K.W.,Wlodawer, A. Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10. J.Mol.Biol., 268:460-467, 1997 Cited by PubMed Abstract: The crystal structure of Epstein-Barr virus protein BCRF1, an analog of cellular interleukin-10 (IL-10), has been determined at the resolution of 1.9 A and refined to an R-factor 0.191. The structure of this cytokine is similar to that of human IL-10 (hIL-10), forming an intercalated dimer of two 17 kDa polypeptides related by a crystallographic 2-fold symmetry axis. BCRF1 exhibits novel conformations of the N-terminal coil and of the loop between helices A and B compared to hIL-10. These regions are likely to be involved in binding of one or more components of the IL-10 receptor system, and thus the structural differences may account for the lower binding affinity and limited spectrum of biological activities of viral IL-10, compared to hIL-10. PubMed: 9159483DOI: 10.1006/jmbi.1997.0990 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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