|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of latent rainbow trout plasminogen activator inhibitor 1 (PAI-1)== | | ==Crystal structure of latent rainbow trout plasminogen activator inhibitor 1 (PAI-1)== |
| - | <StructureSection load='4kds' size='340' side='right' caption='[[4kds]], [[Resolution|resolution]] 1.67Å' scene=''> | + | <StructureSection load='4kds' size='340' side='right'caption='[[4kds]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kds]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncmy Oncmy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KDS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kds]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KDS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6682Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dte|4dte]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">serpine1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8022 ONCMY])</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=4kds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kds OCA], [https://pdbe.org/4kds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kds RCSB], [https://www.ebi.ac.uk/pdbsum/4kds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kds ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kds OCA], [http://pdbe.org/4kds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kds RCSB], [http://www.ebi.ac.uk/pdbsum/4kds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kds ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/I3WWD7_ONCMY I3WWD7_ONCMY] |
| - | 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.
| + | |
| - | | + | |
| - | 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>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4kds" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]] | | *[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Oncmy]] | + | [[Category: Large Structures]] |
| - | [[Category: Johansen, J S]] | + | [[Category: Oncorhynchus mykiss]] |
| - | [[Category: Hydrolase inhibitor]] | + | [[Category: Johansen JS]] |
| - | [[Category: Inactive serpin]]
| + | |
| - | [[Category: Serpin]]
| + | |
| - | [[Category: Trout upa]]
| + | |
