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1adx

From Proteopedia

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{{Seed}}
 
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[[Image:1adx.png|left|200px]]
 
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==FIFTH EGF-LIKE DOMAIN OF THROMBOMODULIN (TMEGF5), NMR, 14 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1adx", creates the "Structure Box" on the page.
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<StructureSection load='1adx' size='340' side='right'caption='[[1adx]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1adx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1adx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adx OCA], [https://pdbe.org/1adx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adx RCSB], [https://www.ebi.ac.uk/pdbsum/1adx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adx ProSAT]</span></td></tr>
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{{STRUCTURE_1adx| PDB=1adx | SCENE= }}
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</table>
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== Disease ==
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===FIFTH EGF-LIKE DOMAIN OF THROMBOMODULIN (TMEGF5), NMR, 14 STRUCTURES===
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[https://www.uniprot.org/uniprot/TRBM_HUMAN TRBM_HUMAN] Defects in THBD are the cause of thrombophilia due to thrombomodulin defect (THPH12) [MIM:[https://omim.org/entry/614486 614486]. A hemostatic disorder characterized by a tendency to thrombosis.<ref>PMID:7811989</ref> <ref>PMID:9198186</ref> <ref>PMID:12139752</ref> Defects in THBD are a cause of susceptibility to hemolytic uremic syndrome atypical type 6 (AHUS6) [MIM:[https://omim.org/entry/612926 612926]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:19625716</ref> <ref>PMID:20513133</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/TRBM_HUMAN TRBM_HUMAN] Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.
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== Evolutionary Conservation ==
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The line below this paragraph, {{ABSTRACT_PUBMED_9367781}}, adds the Publication Abstract to the page
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[[Image:Consurf_key_small.gif|200px|right]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9367781 is the PubMed ID number.
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Check<jmol>
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<jmolCheckbox>
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{{ABSTRACT_PUBMED_9367781}}
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/1adx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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==About this Structure==
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<text>to colour the structure by Evolutionary Conservation</text>
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1ADX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADX OCA].
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</jmolCheckbox>
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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=1adx ConSurf].
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==Reference==
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<div style="clear:both"></div>
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Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern., Sampoli Benitez BA, Hunter MJ, Meininger DP, Komives EA, J Mol Biol. 1997 Nov 7;273(4):913-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9367781 9367781]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hunter, M J.]]
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[[Category: Hunter MJ]]
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[[Category: Komives, E A.]]
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[[Category: Komives EA]]
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[[Category: Meininger, D P.]]
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[[Category: Meininger DP]]
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[[Category: Sampoli-Benitez, B A.]]
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[[Category: Sampoli-Benitez BA]]
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[[Category: Anticoagulant]]
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[[Category: Blood coagulation]]
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[[Category: Disulfide bond]]
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[[Category: Fibrinogen]]
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[[Category: Nmr]]
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[[Category: Peptide synthesis]]
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[[Category: Protein c]]
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[[Category: Thrombin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:38:48 2008''
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Current revision

FIFTH EGF-LIKE DOMAIN OF THROMBOMODULIN (TMEGF5), NMR, 14 STRUCTURES

PDB ID 1adx

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