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1as4

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CLEAVED ANTICHYMOTRYPSIN A349R

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Retrieved from "http://52.214.119.220/wiki/index.php/1as4"

Categories: Homo sapiens | Large Structures | Christianson DW | Lukacs CM

@@ Line 1: / Line 1: @@
-[[Image:1as4.gif|left|200px]]<br />
-<applet load="1as4" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1as4, resolution 2.1&Aring;" />
-'''CLEAVED ANTICHYMOTRYPSIN A349R'''<br />
-==Overview==
+==CLEAVED ANTICHYMOTRYPSIN A349R==
-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.
+<StructureSection load='1as4' size='340' side='right'caption='[[1as4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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>
+== 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/as/1as4_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=1as4 ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known diseases 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]]
+*[[Serpin 3D structures|Serpin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-AS4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AS4 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9521649 9521649]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Christianson, D.W.]]
+[[Category: Christianson DW]]
-[[Category: Lukacs, C.M.]]
+[[Category: Lukacs CM]]
-[[Category: ACT]]
-[[Category: antichymotrypsin]]
-[[Category: serine protease inhibitor]]
-[[Category: serpin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:01:30 2007''

1as4

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CLEAVED ANTICHYMOTRYPSIN A349R

Structural highlights

Function

Evolutionary Conservation

See Also

References

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