3bt2: Difference between revisions

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[[Image:3bt2.png|left|200px]]


{{STRUCTURE_3bt2| PDB=3bt2 | SCENE= }}
==Structure of urokinase receptor, urokinase and vitronectin complex==
<StructureSection load='3bt2' size='340' side='right'caption='[[3bt2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bt2]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BT2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bt2 OCA], [https://pdbe.org/3bt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bt2 RCSB], [https://www.ebi.ac.uk/pdbsum/3bt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bt2 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[https://omim.org/entry/601709 601709]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
== Function ==
[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
== 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/bt/3bt2_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=3bt2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The urokinase receptor (uPAR) can recognize several ligands. The structural basis for this multiple ligand recognition by uPAR is unknown. This study reports the crystal structures of uPAR in complex with both urokinase (uPA) and vitronectin and reveal that uPA occupies the central cavity of the receptor, whereas vitronectin binds at the outer side of the receptor. These results provide a structural understanding of one receptor binding to two ligands.


===Structure of urokinase receptor, urokinase and vitronectin complex===
Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes.,Huai Q, Zhou A, Lin L, Mazar AP, Parry GC, Callahan J, Shaw DE, Furie B, Furie BC, Huang M Nat Struct Mol Biol. 2008 Apr;15(4):422-3. Epub 2008 Mar 23. PMID:18376415<ref>PMID:18376415</ref>


{{ABSTRACT_PUBMED_18376415}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3bt2" style="background-color:#fffaf0;"></div>
[[3bt2]] is a 5 chain structure of [[Urokinase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BT2 OCA].


==See Also==
==See Also==
*[[Urokinase|Urokinase]]
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[Urokinase 3D Structures|Urokinase 3D Structures]]
==Reference==
*[[3D structures of human antibody|3D structures of human antibody]]
<ref group="xtra">PMID:018376415</ref><references group="xtra"/>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Huang, M.]]
[[Category: Huang M]]
[[Category: Blood coagulation]]
[[Category: Cell adhesion]]
[[Category: Egf-like domain]]
[[Category: Fibrinolysis]]
[[Category: Glycoprotein]]
[[Category: Gpi-anchor]]
[[Category: Heparin-binding]]
[[Category: Hydrolase]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Kringle]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Phosphoprotein]]
[[Category: Plasminogen activation]]
[[Category: Protease]]
[[Category: Protein-protein interaction]]
[[Category: Receptor]]
[[Category: Secreted]]
[[Category: Serine protease]]
[[Category: Sulfation]]
[[Category: Zymogen]]

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