3evj
From Proteopedia
(Difference between revisions)
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- | + | ==Intermediate structure of antithrombin bound to the natural pentasaccharide== | |
- | + | <StructureSection load='3evj' size='340' side='right' caption='[[3evj]], [[Resolution|resolution]] 3.00Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3evj]] is a 2 chain structure with 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=3EVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVJ FirstGlance]. <br> | |
- | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NTO:TRISULFOAMINO+HEPARIN+PENTASACCHARIDE'>NTO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
- | [[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref>[:]<ref>PMID:3191114</ref><ref>PMID:9031473</ref><ref>PMID:6582486</ref><ref>PMID:3080419</ref><ref>PMID:3805013</ref><ref>PMID:3179438</ref><ref>PMID:3162733</ref><ref>PMID:2781509</ref><ref>PMID:2365065</ref><ref>PMID:2229057</ref><ref>PMID:2013320</ref><ref>PMID:1906811</ref><ref>PMID:1555650</ref><ref>PMID:1547341</ref><ref>PMID:8443391</ref><ref>PMID:8486379</ref><ref>PMID:7981186</ref><ref>PMID:7959685</ref><ref>PMID:8274732</ref><ref>PMID:7994035</ref><ref>PMID:7989582</ref>[:]<ref>PMID:7878627</ref><ref>PMID:7832187</ref><ref>PMID:9157604</ref><ref>PMID:9845533</ref><ref>PMID:9759613</ref><ref>PMID:10997988</ref><ref>PMID:11794707</ref><ref>PMID:11713457</ref><ref>PMID:12353073</ref><ref>PMID:12595305</ref><ref>PMID:12894857</ref><ref>PMID:15164384</ref><ref>PMID:16908819</ref> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nq9|1nq9]], [[2b5t|2b5t]]</td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3evj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3evj RCSB], [http://www.ebi.ac.uk/pdbsum/3evj PDBsum]</span></td></tr> | |
- | ==Function== | + | </table> |
- | [[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref> | + | == Disease == |
- | + | [[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref> | |
- | == | + | == Function == |
- | [[ | + | [[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</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/ev/3evj_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Antithrombin|Antithrombin]] | *[[Antithrombin|Antithrombin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Belzar, K J | + | [[Category: Belzar, K J]] |
- | [[Category: Huntington, J A | + | [[Category: Huntington, J A]] |
[[Category: Blood coagulation]] | [[Category: Blood coagulation]] | ||
[[Category: Disease mutation]] | [[Category: Disease mutation]] |
Revision as of 13:21, 18 December 2014
Intermediate structure of antithrombin bound to the natural pentasaccharide
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