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New page: '''Unreleased structure''' The entry 2kmq is ON HOLD Authors: Pantoja-Uceda, D., Santoro, J. Description: Solution structure of intermediate IIb of Leech-derived tryptase inhibitor, LD... |
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The | ==Solution structure of intermediate IIb of Leech-derived tryptase inhibitor, LDTI.== | ||
<StructureSection load='2kmq' size='340' side='right'caption='[[2kmq]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kmq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KMQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2kmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kmq OCA], [https://pdbe.org/2kmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kmq RCSB], [https://www.ebi.ac.uk/pdbsum/2kmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kmq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LDTI_HIRME LDTI_HIRME] Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms. | |||
== 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/km/2kmq_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2kmq ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein folding mechanisms have remained elusive mainly because of the transient nature of intermediates. Leech-derived tryptase inhibitor (LDTI) is a Kazal-type serine proteinase inhibitor that is emerging as an attractive model for folding studies. It comprises 46 amino acid residues with three disulfide bonds, with one located inside a small triple-stranded antiparallel beta-sheet and with two involved in a cystine-stabilized alpha-helix, a motif that is widely distributed in bioactive peptides. Here, we analyzed the oxidative folding and reductive unfolding of LDTI by chromatographic and disulfide analyses of acid-trapped intermediates. It folds and unfolds, respectively, via sequential oxidation and reduction of the cysteine residues that give rise to a few 1- and 2-disulfide intermediates. Species containing two native disulfide bonds predominate during LDTI folding (IIa and IIc) and unfolding (IIa and IIb). Stop/go folding experiments demonstrate that only intermediate IIa is productive and oxidizes directly into the native form. The NMR structures of acid-trapped and further isolated IIa, IIb, and IIc reveal global folds similar to that of the native protein, including a native-like canonical inhibitory loop. Enzyme kinetics shows that both IIa and IIc are inhibitory-active, which may substantially reduce proteolysis of LDTI during its folding process. The results reported show that the kinetics of the folding reaction is modulated by the specific structural properties of the intermediates and together provide insights into the interdependence of conformational folding and the assembly of native disulfides during oxidative folding. | |||
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.,Pantoja-Uceda D, Arolas JL, Aviles FX, Santoro J, Ventura S, Sommerhoff CP J Biol Chem. 2009 Dec 18;284(51):35612-20. Epub . PMID:19820233<ref>PMID:19820233</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kmq" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tryptase inhibitor|Tryptase inhibitor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hirudo medicinalis]] | |||
[[Category: Large Structures]] | |||
[[Category: Pantoja-Uceda D]] | |||
[[Category: Santoro J]] | |||