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.
1inr
From Proteopedia
|
CYTOKINE SYNTHESIS
Contents |
Overview
The crystal structure of recombinant human interleukin 10 (rhIL-10) has, been determined by X-ray crystallography at 2.0 A resolution. Interleukin, 10 is a dimer composed of identical polypeptide chains related by a 2-fold, axis. The molecule is predominantly alpha-helical. The main-chain fold, resembles that of interferon gamma (IFN-gamma) in which the structural, integrity of each domain is dependent on the intertwining of helices from, each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals, differences in helix lengths and orientations of the 2-fold related, domains. Interleukin 10 and IFN-gamma contain several conserved residues, in their internal cores which suggest a possible "fingerprint" for, detection of other members of this fold.
Disease
Known diseases associated with this structure: Graft-versus-host disease, protection against OMIM:[124092], HIV-1, susceptibility to OMIM:[124092], Rheumatoid arthritis, progression of OMIM:[124092]
About this Structure
1INR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of interleukin 10 reveals an interferon gamma-like fold., Walter MR, Nagabhushan TL, Biochemistry. 1995 Sep 26;34(38):12118-25. PMID:7547951
Page seeded by OCA on Mon Nov 12 17:32:07 2007
