3caa: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3caa.png|left|200px]]
-<!--
+==CLEAVED ANTICHYMOTRYPSIN A347R==
-The line below this paragraph, containing "STRUCTURE_3caa", creates the "Structure Box" on the page.
+<StructureSection load='3caa' size='340' side='right'caption='[[3caa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3caa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2caa 2caa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=3caa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3caa OCA], [https://pdbe.org/3caa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3caa RCSB], [https://www.ebi.ac.uk/pdbsum/3caa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3caa ProSAT]</span></td></tr>
-{{STRUCTURE_3caa|  PDB=3caa  |  SCENE=  }}
+</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/ca/3caa_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=3caa ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===CLEAVED ANTICHYMOTRYPSIN A347R===
+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:9521649<ref>PMID:9521649</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3caa" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8836107}}, adds the Publication Abstract to the page
+*[[Serpin 3D structures|Serpin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8836107 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8836107}}
+__TOC__
+</StructureSection>
-==Disease==
-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]]
-==About this Structure==
-CAA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2caa 2caa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAA OCA].
-==Reference==
-Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement., Lukacs CM, Zhong JQ, Plotnick MI, Rubin H, Cooperman BS, Christianson DW, Nat Struct Biol. 1996 Oct;3(10):888-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8836107 8836107]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Christianson, D W.]]
+[[Category: Christianson DW]]
-[[Category: Lukacs, C M.]]
+[[Category: Lukacs CM]]
-[[Category: Antichymotrypsin]]
-[[Category: Serine protease inhibitor]]
-[[Category: Serpin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:37:48 2008''