This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1qrz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1qrz" [edit=sysop:move=sysop])
Current revision (06:06, 17 April 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1qrz.png|left|200px]]
 
-
{{STRUCTURE_1qrz| PDB=1qrz | SCENE= }}
+
==CATALYTIC DOMAIN OF PLASMINOGEN==
-
 
+
<StructureSection load='1qrz' size='340' side='right'caption='[[1qrz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
===CATALYTIC DOMAIN OF PLASMINOGEN===
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[1qrz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRZ FirstGlance]. <br>
-
{{ABSTRACT_PUBMED_10460175}}
+
</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&#8491;</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=1qrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrz OCA], [https://pdbe.org/1qrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qrz RCSB], [https://www.ebi.ac.uk/pdbsum/1qrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qrz ProSAT]</span></td></tr>
-
==About this Structure==
+
</table>
-
[[1qrz]] is a 4 chain structure of [[Plasminogen]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRZ OCA].
+
== Disease ==
 +
[https://www.uniprot.org/uniprot/PLMN_HUMAN PLMN_HUMAN] Defects in PLG are the cause of plasminogen deficiency (PLGD) [MIM:[https://omim.org/entry/217090 217090]. PLGD is characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa.<ref>PMID:1986355</ref> <ref>PMID:8392398</ref> <ref>PMID:6216475</ref> <ref>PMID:6238949</ref> <ref>PMID:1427790</ref> <ref>PMID:9242524</ref> <ref>PMID:9858247</ref> <ref>PMID:10233898</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PLMN_HUMAN PLMN_HUMAN] Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.<ref>PMID:14699093</ref> Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.<ref>PMID:14699093</ref>
 +
== 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/qr/1qrz_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=1qrz ConSurf].
 +
<div style="clear:both"></div>
==See Also==
==See Also==
-
*[[Plasminogen|Plasminogen]]
+
*[[Plasminogen 3D structures|Plasminogen 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:010460175</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Peisach, E.]]
+
[[Category: Large Structures]]
-
[[Category: Reich, E.]]
+
[[Category: Peisach E]]
-
[[Category: Ringe, D.]]
+
[[Category: Reich E]]
-
[[Category: Santos, T de los.]]
+
[[Category: Ringe D]]
-
[[Category: Wang, J.]]
+
[[Category: Wang J]]
-
[[Category: Chymotrypsin family]]
+
[[Category: De los Santos T]]
-
[[Category: Hydrolase]]
+
-
[[Category: Microplasminogen]]
+
-
[[Category: Serine protease]]
+
-
[[Category: Zymogen]]
+

Current revision

CATALYTIC DOMAIN OF PLASMINOGEN

PDB ID 1qrz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools