1hig
From Proteopedia
(Difference between revisions)
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<StructureSection load='1hig' size='340' side='right'caption='[[1hig]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1hig' size='340' side='right'caption='[[1hig]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1hig]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HIG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hig]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HIG FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hig OCA], [https://pdbe.org/1hig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hig RCSB], [https://www.ebi.ac.uk/pdbsum/1hig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hig ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hig OCA], [https://pdbe.org/1hig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hig RCSB], [https://www.ebi.ac.uk/pdbsum/1hig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hig ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | + | [https://www.uniprot.org/uniprot/IFNG_HUMAN IFNG_HUMAN] In Caucasians, genetic variation in IFNG is associated with the risk of aplastic anemia (AA) [MIM:[https://omim.org/entry/609135 609135]. AA is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis. | |
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/IFNG_HUMAN IFNG_HUMAN] Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hig ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hig ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is primarily alpha helical, with six helices in each subunit that comprise approximately 62 percent of the structure; there is no beta sheet. The dimeric structure of human interferon-gamma is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions. | ||
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| - | Three-dimensional structure of recombinant human interferon-gamma.,Ealick SE, Cook WJ, Vijay-Kumar S, Carson M, Nagabhushan TL, Trotta PP, Bugg CE Science. 1991 May 3;252(5006):698-702. PMID:1902591<ref>PMID:1902591</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1hig" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Interferon 3D structures|Interferon 3D structures]] | *[[Interferon 3D structures|Interferon 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bugg | + | [[Category: Bugg CE]] |
| - | [[Category: Carson | + | [[Category: Carson M]] |
| - | [[Category: Cook | + | [[Category: Cook WJ]] |
| - | [[Category: Ealick | + | [[Category: Ealick SE]] |
| - | [[Category: Nagabhushan | + | [[Category: Nagabhushan TL]] |
| - | [[Category: Trotta | + | [[Category: Trotta PP]] |
| - | [[Category: Vijay-Kumar | + | [[Category: Vijay-Kumar S]] |
| - | + | ||
Current revision
THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT HUMAN INTERFERON-GAMMA.
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