1as4

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[[Image:1as4.jpg|left|200px]]
 
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{{Structure
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==CLEAVED ANTICHYMOTRYPSIN A349R==
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|PDB= 1as4 |SIZE=350|CAPTION= <scene name='initialview01'>1as4</scene>, resolution 2.1&Aring;
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<StructureSection load='1as4' size='340' side='right'caption='[[1as4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>
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<table><tr><td colspan='2'>[[1as4]] is a 2 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=1AS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AS4 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.1&#8491;</td></tr>
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|GENE= ACT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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|DOMAIN=
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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=1as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1as4 OCA], [https://pdbe.org/1as4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1as4 RCSB], [https://www.ebi.ac.uk/pdbsum/1as4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1as4 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1as4 OCA], [http://www.ebi.ac.uk/pdbsum/1as4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1as4 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AACT_HUMAN AACT_HUMAN] Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.<ref>PMID:2404007</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/as/1as4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1as4 ConSurf].
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<div style="clear:both"></div>
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'''CLEAVED ANTICHYMOTRYPSIN A349R'''
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==See Also==
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*[[Serpin 3D structures|Serpin 3D structures]]
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== References ==
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==Overview==
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<references/>
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Expressed in a kinetically trapped folding state, a serpin couples the thermodynamic driving force of a massive beta-sheet rearrangement to the inhibition of a target protease. Hence, the serpin-protease interaction is the premier example of a "spring-loaded" protein-protein interaction. Amino acid substitutions in the hinge region of a serpin reactive loop can weaken the molecular spring, which converts the serpin from an inhibitor into a substrate. To probe the molecular basis of this conversion, we report the crystal structure of A349R antichymotrypsin in the reactive loop cleaved state at 2.1 A resolution. This amino acid substitution does not block the beta-sheet rearrangement despite the burial of R349 in the hydrophobic core of the cleaved serpin along with a salt-linked acetate ion. The inhibitory activity of this serpin variant is not obliterated; remarkably, its inhibitory properties are anion-dependent due to the creation of an anion-binding cavity in the cleaved serpin.
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Alpha-1-antichymotrypsin deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107280 107280]], Cerebrovascular disease, occlusive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107280 107280]]
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==About this Structure==
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1AS4 is a [[Protein complex]] structure of sequences 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=1AS4 OCA].
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==Reference==
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Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction., Lukacs CM, Rubin H, Christianson DW, Biochemistry. 1998 Mar 10;37(10):3297-304. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9521649 9521649]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Christianson, D W.]]
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[[Category: Christianson DW]]
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[[Category: Lukacs, C M.]]
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[[Category: Lukacs CM]]
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[[Category: antichymotrypsin]]
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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 Sun Mar 30 18:46:30 2008''
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Current revision

CLEAVED ANTICHYMOTRYPSIN A349R

PDB ID 1as4

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