2ilk: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION== | ==CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION== | ||
<StructureSection load='2ilk' size='340' side='right' caption='[[2ilk]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2ilk' size='340' side='right'caption='[[2ilk]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ilk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ilk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ilk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilk OCA], [https://pdbe.org/2ilk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ilk RCSB], [https://www.ebi.ac.uk/pdbsum/2ilk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ilk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/IL10_HUMAN IL10_HUMAN]] Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Interleukin|Interleukin]] | *[[Interleukin 3D structures|Interleukin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Schalk-Hihi, C]] | [[Category: Schalk-Hihi, C]] | ||
[[Category: Wlodawer, A]] | [[Category: Wlodawer, A]] | ||
[[Category: Zdanov, A]] | [[Category: Zdanov, A]] | ||
[[Category: Cytokine]] | [[Category: Cytokine]] | ||
Latest revision as of 13:29, 12 January 2022
CRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF HUMAN INTERLEUKIN-10 AT 1.6 ANGSTROMS RESOLUTION
Structural highlights
Function[IL10_HUMAN] Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||