3bt2: Difference between revisions

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


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==Structure of urokinase receptor, urokinase and vitronectin complex==
The line below this paragraph, containing "STRUCTURE_3bt2", creates the "Structure Box" on the page.
<StructureSection load='3bt2' size='340' side='right'caption='[[3bt2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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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]] 2.5&#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>
{{STRUCTURE_3bt2| PDB=3bt2  | SCENE= }}
<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>
'''Structure of urokinase receptor, urokinase and vitronectin complex'''
== 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 ==
==Overview==
[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>
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    <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].
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== 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.
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.


==Disease==
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>
Known disease associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191840 191840]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3BT2 is a [[Protein complex]] structure of sequences 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].
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<div class="pdbe-citations 3bt2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18376415 18376415]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Urokinase 3D Structures|Urokinase 3D Structures]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Huang M]]
[[Category: Huang, M.]]
[[Category: Alternative splicing]]
[[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: Pharmaceutical]]
[[Category: Phosphoprotein]]
[[Category: Plasminogen activation]]
[[Category: Polymorphism]]
[[Category: Protease]]
[[Category: Protein-protein interaction]]
[[Category: Receptor]]
[[Category: Secreted]]
[[Category: Serine protease]]
[[Category: Sulfation]]
[[Category: Zymogen]]
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