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New page: left|200px<br /> <applet load="1z2m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z2m, resolution 2.50Å" /> '''Crystal Structure o...
 
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[[Image:1z2m.gif|left|200px]]<br />
<applet load="1z2m" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1z2m, resolution 2.50&Aring;" />
'''Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein'''<br />


==Overview==
==Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein==
The biological effects of the ISG15 protein arise in part from its, conjugation to cellular targets as a primary response to, interferon-alpha/beta induction and other markers of viral or parasitic, infection. Recombinant full-length ISG15 has been produced for the first, time in high yield by mutating Cys78 to stabilize the protein and by, cloning in a C-terminal arginine cap to protect the C terminus against, proteolytic inactivation. The cap is subsequently removed with, carboxypeptidase B to yield mature biologically active ISG15 capable of, stoichiometric ATP-dependent thiolester formation with its human UbE1L, activating enzyme. The three-dimensional structure of recombinant, ISG15C78S was determined at 2.4-A resolution. The ISG15 structure, comprises two beta-grasp folds having main chain root mean square, deviation (r.m.s.d.) values from ubiquitin of 1.7 A (N-terminal) and 1.0 A, (C-terminal). The beta-grasp domains pack across two conserved 3(10), helices to bury 627 A2 that accounts for 7% of the total, solvent-accessible surface area. The distribution of ISG15 surface charge, forms a ridge of negative charge extending nearly the full-length of the, molecule. Additionally, the N-terminal domain contains an apolar region, comprising almost half its solvent accessible surface. The C-terminal, domain of ISG15 was superimposed on the structure of Nedd8 (r.m.s.d. =, 0.84 A) bound to its AppBp1-Uba3 activating enzyme to model ISG15 binding, to UbE1L. The docking model predicts several key side-chain interactions, that presumably define the specificity between the ubiquitin and ISG15, ligation pathways to maintain functional integrity of their signaling.
<StructureSection load='1z2m' size='340' side='right'caption='[[1z2m]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1z2m]] is a 1 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=1Z2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2M FirstGlance]. <br>
1Z2M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with OS4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z2M OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OS4:OSMIUM+4++ION'>OS4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2m OCA], [https://pdbe.org/1z2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z2m RCSB], [https://www.ebi.ac.uk/pdbsum/1z2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2m ProSAT]</span></td></tr>
Crystal structure of the interferon-induced ubiquitin-like protein ISG15., Narasimhan J, Wang M, Fu Z, Klein JM, Haas AL, Kim JJ, J Biol Chem. 2005 Jul 22;280(29):27356-65. Epub 2005 May 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15917233 15917233]
</table>
== Function ==
[https://www.uniprot.org/uniprot/ISG15_HUMAN ISG15_HUMAN] Ubiquitin-like protein that is conjugated to intracellular target proteins after IFN-alpha or IFN-beta stimulation. Its enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the Ub conjugation pathway at the level of a specific E2 enzyme. Targets include STAT1, SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MxA, and RIG-1. Deconjugated by USP18/UBP43. Shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. May serve as a trans-acting binding factor directing the association of ligated target proteins to intermediate filaments. May also be involved in autocrine, paracrine and endocrine mechanisms, as in cell-to-cell signaling, possibly partly by inducing IFN-gamma secretion by monocytes and macrophages. Seems to display antiviral activity during viral infections.<ref>PMID:1373138</ref> <ref>PMID:7526157</ref> <ref>PMID:8550581</ref> <ref>PMID:2005397</ref> <ref>PMID:16254333</ref> <ref>PMID:16009940</ref>  In response to IFN-tau secreted by the conceptus, may ligate to and regulate proteins involved in the release of prostaglandin F2-alpha (PGF), and thus prevent lysis of the corpus luteum and maintain the pregnancy (By similarity).<ref>PMID:1373138</ref> <ref>PMID:7526157</ref> <ref>PMID:8550581</ref> <ref>PMID:2005397</ref> <ref>PMID:16254333</ref> <ref>PMID:16009940</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/1z2m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1z2m ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fu, Z.]]
[[Category: Fu Z]]
[[Category: Haas, A.L.]]
[[Category: Haas AL]]
[[Category: Kim, J.J.]]
[[Category: Kim JJ]]
[[Category: Klein, J.M.]]
[[Category: Klein JM]]
[[Category: Narasimhan, J.]]
[[Category: Narasimhan J]]
[[Category: Wang, M.]]
[[Category: Wang M]]
[[Category: OS4]]
[[Category: isg15]]
[[Category: ubiquitin cross reactive protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:28:36 2007''

Latest revision as of 09:02, 14 February 2024

Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein

1z2m, resolution 2.50Å

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