5lhs: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The ligand free catalytic domain of murine urokinase-type plasminogen activator== | ==The ligand free catalytic domain of murine urokinase-type plasminogen activator== | ||
<StructureSection load='5lhs' size='340' side='right' caption='[[5lhs]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='5lhs' size='340' side='right'caption='[[5lhs]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lhs]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5lhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LHS FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.047Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5lhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhs OCA], [https://pdbe.org/5lhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lhs RCSB], [https://www.ebi.ac.uk/pdbsum/5lhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhs ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/UROK_MOUSE UROK_MOUSE] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5lhs" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5lhs" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Plasminogen activator|Plasminogen activator]] | |||
*[[Urokinase 3D Structures|Urokinase 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Andreasen | [[Category: Andreasen PA]] | ||
[[Category: Declerck | [[Category: Declerck PJ]] | ||
[[Category: Ghassabeh | [[Category: Ghassabeh GH]] | ||
[[Category: Huang | [[Category: Huang M]] | ||
[[Category: Jensen | [[Category: Jensen JK]] | ||
[[Category: Kromann-Hansen | [[Category: Kromann-Hansen T]] | ||
[[Category: Lange | [[Category: Lange EL]] | ||
[[Category: Muyldermans | [[Category: Muyldermans S]] | ||
[[Category: Sorensen | [[Category: Sorensen HP]] | ||
Latest revision as of 21:26, 18 October 2023
The ligand free catalytic domain of murine urokinase-type plasminogen activatorThe ligand free catalytic domain of murine urokinase-type plasminogen activator
Structural highlights
FunctionUROK_MOUSE Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. Publication Abstract from PubMedAlthough trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the different conformations have remained largely obscure. The trypsin-like serine protease, urokinase-type plasminogen activator (uPA), is central in tissue remodeling processes and also strongly implicated in tumor metastasis. We solved five X-ray crystal structures of murine uPA (muPA) in the absence and presence of allosteric molecules and/or substrate-like molecules. The structure of unbound muPA revealed an unsuspected non-chymotrypsin-like protease conformation in which two beta-strands in the core of the protease domain undergoes a major antiparallel-to-parallel conformational transition. We next isolated two anti-muPA nanobodies; an active-site binding nanobody and an allosteric nanobody. Crystal structures of the muPA:nanobody complexes and hydrogen-deuterium exchange mass spectrometry revealed molecular insights about molecular factors controlling the antiparallel-to-parallel equilibrium in muPA. Together with muPA activity assays, the data provide valuable insights into regulatory mechanisms and conformational flexibility of uPA and trypsin-like serine proteases in general. Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator.,Kromann-Hansen T, Louise Lange E, Peter Sorensen H, Hassanzadeh-Ghassabeh G, Huang M, Jensen JK, Muyldermans S, Declerck PJ, Komives EA, Andreasen PA Sci Rep. 2017 Jun 13;7(1):3385. doi: 10.1038/s41598-017-03457-7. PMID:28611361[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||