This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1vlk
From Proteopedia
|
STRUCTURE OF VIRAL INTERLEUKIN-10
Overview
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.
About this Structure
1VLK is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10., Zdanov A, Schalk-Hihi C, Menon S, Moore KW, Wlodawer A, J Mol Biol. 1997 May 2;268(2):460-7. PMID:9159483
Page seeded by OCA on Wed Nov 21 04:56:20 2007
