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4dte

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Current revision (14:44, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DTE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DTE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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]] 1.96&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4dte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dte OCA], [https://pdbe.org/4dte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dte RCSB], [https://www.ebi.ac.uk/pdbsum/4dte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dte ProSAT]</span></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=4dte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dte OCA], [https://pdbe.org/4dte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dte RCSB], [https://www.ebi.ac.uk/pdbsum/4dte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dte ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/F1QRB8_DANRE F1QRB8_DANRE]]
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[https://www.uniprot.org/uniprot/F1QRB8_DANRE F1QRB8_DANRE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Very few studies have attributed a direct, active, functional role to N-linked glycans. We describe here an N-linked glycan with a unique role for maintaining the active conformation of a protein of the serpin family. The distinguishing feature of serpins is the "stressed-to-relaxed" transition, in which the reactive center loop inserts as a beta-strand into the central beta-sheet A. This transition forms the basis for the conversion of serpins to the inactive latent state. We demonstrate that plasminogen activator inhibitor-1 (PAI-1) from zebrafish converts to the latent state about 5-fold slower than human PAI-1. In contrast to human PAI-1, fish PAI-1 carries a single N-linked glycan at Asn185 in the gate region through which the reactive center loop passes during latency transition. While the latency transition of human PAI-1 is unaffected by deglycosylation, deglycosylated zebrafish PAI-1 (zfPAI-1) goes latent about 50-fold faster than the glycosylated zfPAI-1 and about 25-fold faster than non-glycosylated human PAI-1. X-ray crystal structure analysis of glycosylated fish PAI-1 confirmed the presence of an N-linked glycan in the gate region and a lack of glycan-induced structural changes. Thus, latency transition of zfPAI-1 is delayed by steric hindrance from the glycan in the gate region. Our findings reveal a previously unknown mechanism for inhibition of protein conformational changes by steric hindrance from N-linked glycans.
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Protein conformational change delayed by steric hindrance from an N-linked glycan.,Bager R, Johansen JS, Jensen JK, Stensballe A, Jendroszek A, Buxbom L, Sorensen HP, Andreasen PA J Mol Biol. 2013 Aug 23;425(16):2867-77. doi: 10.1016/j.jmb.2013.05.007. Epub, 2013 May 20. PMID:23702291<ref>PMID:23702291</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 4dte" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]]
*[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of zebrafish plasminogen activator inhibitor-1 (PAI-1)

PDB ID 4dte

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