2ilk
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION
Contents |
Overview
The crystal structure of human interleukin-10 (IL-10) was refined at 1.6 A, resolution against X-ray diffraction data collected at 100 K with the use, of synchrotron radiation. Although similar to the IL-10 structure, determined previously at room temperature, this low-temperature IL-10, structure contains, in addition, four N-terminal residues, three sulfate, anions, and 175 extra water molecules. Whereas the main-chain conformation, is preserved, about 30% of the side chains, most of them on the protein, surface, assume different conformations. A computer model of a complex of, IL-10 with its two soluble receptors was generated based on the, topological similarity of IL-10 to interferon-gamma. The contact region, between the cytokine and each receptor shows excellent complementarity of, polar and hydrophobic interactions, suggesting that the model is generally, correct and should be useful in guiding mutagenesis experiments.
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
2ILK is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor., Zdanov A, Schalk-Hihi C, Wlodawer A, Protein Sci. 1996 Oct;5(10):1955-62. PMID:8897595
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