3cwl

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{{Seed}}
 
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[[Image:3cwl.png|left|200px]]
 
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==Crystal structure of alpha-1-antitrypsin, crystal form B==
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The line below this paragraph, containing "STRUCTURE_3cwl", creates the "Structure Box" on the page.
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<StructureSection load='3cwl' size='340' side='right'caption='[[3cwl]], [[Resolution|resolution]] 2.44&Aring;' 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'>[[3cwl]] 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=3CWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CWL 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">X-ray diffraction, [[Resolution|Resolution]] 2.44&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
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{{STRUCTURE_3cwl| PDB=3cwl | SCENE= }}
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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=3cwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cwl OCA], [https://pdbe.org/3cwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cwl RCSB], [https://www.ebi.ac.uk/pdbsum/3cwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cwl ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[https://omim.org/entry/613490 613490]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cw/3cwl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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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=3cwl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The aggregation of antitrypsin into polymers is one of the causes of neonatal hepatitis, cirrhosis, and emphysema. A similar reaction resulting in disease can occur in other human serpins, and collectively they are known as the serpinopathies. One possible therapeutic strategy involves inhibiting the conformational changes involved in antitrypsin aggregation. The citrate ion has previously been shown to prevent antitrypsin aggregation and maintain the protein in an active conformation; its mechanism of action, however, is unknown. Here we demonstrate that the citrate ion prevents the initial misfolding of the native state to a polymerogenic intermediate in a concentration-dependent manner. Furthermore, we have solved the crystal structure of citrate bound to antitrypsin and show that a single citrate molecule binds in a pocket between the A and B beta-sheets, a region known to be important in maintaining antitrypsin stability.
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===Crystal structure of alpha-1-antitrypsin, crystal form B===
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Preventing serpin aggregation: the molecular mechanism of citrate action upon antitrypsin unfolding.,Pearce MC, Morton CJ, Feil SC, Hansen G, Adams JJ, Parker MW, Bottomley SP Protein Sci. 2008 Dec;17(12):2127-33. Epub 2008 Sep 9. PMID:18780818<ref>PMID:18780818</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3cwl" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18780818}}, adds the Publication Abstract to the page
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*[[Alpha-1-antitrypsin 3D structures|Alpha-1-antitrypsin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18780818 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18780818}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3CWL is a 1 chain structure of 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=3CWL OCA].
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==Reference==
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<ref group="xtra">PMID:18780818</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Adams, J J.]]
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[[Category: Large Structures]]
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[[Category: Feil, S C.]]
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[[Category: Adams JJ]]
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[[Category: Hansen, G.]]
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[[Category: Feil SC]]
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[[Category: Morton, C J.]]
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[[Category: Hansen G]]
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[[Category: Parker, M W.]]
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[[Category: Morton CJ]]
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[[Category: Acute phase]]
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[[Category: Parker MW]]
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[[Category: Alternative splicing]]
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[[Category: Antitrypsin]]
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[[Category: Blood coagulation]]
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[[Category: Disease mutation]]
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[[Category: Glycoprotein]]
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[[Category: Polymerisation]]
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[[Category: Polymorphism]]
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[[Category: Protease inhbitor]]
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[[Category: Protein aggregation]]
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[[Category: Protein unfolding]]
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[[Category: Secreted]]
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[[Category: Serine protease inhibitor]]
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[[Category: Serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:45:42 2009''
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Current revision

Crystal structure of alpha-1-antitrypsin, crystal form B

PDB ID 3cwl

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