2ilk: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2ilk.jpg|left|200px]] | [[Image:2ilk.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 2ilk |SIZE=350|CAPTION= <scene name='initialview01'>2ilk</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
2ILK is a [ | 2ILK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILK OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8897595 8897595] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 22: | Line 31: | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:30:53 2008'' |
Revision as of 18:30, 20 March 2008
| |||||||
, resolution 1.6Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION
OverviewOverview
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.
DiseaseDisease
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 StructureAbout this Structure
2ILK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Mar 20 17:30:53 2008