2ol2: Difference between revisions

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-[[Image:2ol2.png|left|200px]]
-<!--
+==High Resolution Structure of Native PCI in Space Group P21==
-The line below this paragraph, containing "STRUCTURE_2ol2", creates the "Structure Box" on the page.
+<StructureSection load='2ol2' size='340' side='right'caption='[[2ol2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ol2]] is a 2 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=2OL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OL2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_2ol2|  PDB=2ol2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ol2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol2 OCA], [https://pdbe.org/2ol2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ol2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ol2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ol2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IPSP_HUMAN IPSP_HUMAN] Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.<ref>PMID:6323392</ref> <ref>PMID:3501295</ref> <ref>PMID:2844223</ref> <ref>PMID:1725227</ref> <ref>PMID:7521127</ref> <ref>PMID:7548057</ref> <ref>PMID:8536714</ref> <ref>PMID:8665956</ref> <ref>PMID:9473218</ref> <ref>PMID:9510955</ref> <ref>PMID:9556620</ref> <ref>PMID:10340997</ref> <ref>PMID:11722589</ref> <ref>PMID:14696115</ref> <ref>PMID:15328353</ref> <ref>PMID:15140131</ref> <ref>PMID:15853774</ref> <ref>PMID:18467335</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/ol/2ol2_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=2ol2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein C inhibitor (PCI) is a multifunctional serpin with wide ranging protease inhibitory functions, unique cofactor binding activities, and potential non-inhibitory functions akin to the hormone-transporting serpins. To gain insight into the molecular mechanisms utilized by PCI we developed a robust expression system in Escherichia coli and solved the crystal structure of PCI in its native state. The five monomers obtained from our two crystal forms provide an NMR-like ensemble revealing regions of inherent flexibility. The reactive center loop (RCL) of PCI is long and highly flexible with no evidence of hinge region incorporation into beta-sheet A, as seen for other heparin-binding serpins. We adapted an extrinsic fluorescence method for determining dissociation constants for heparin and find that the N-terminal tail of PCI and residues adjacent to helix H are not involved in heparin binding. The minimal heparin length capable of tight binding to PCI was determined to be chains of eight monosaccharide units. A large hydrophobic pocket occupied by hydrophobic crystal contacts was found in an analogous position to the hormone-binding site in thyroxine-binding globulin. In conclusion, the data presented here provide important insights into the mechanisms by which PCI exercises its multiple inhibitory and non-inhibitory functions.
-===High Resolution Structure of Native PCI in Space Group P21===
+Structure of native protein C inhibitor provides insight into its multiple functions.,Li W, Adams TE, Kjellberg M, Stenflo J, Huntington JA J Biol Chem. 2007 May 4;282(18):13759-68. Epub 2007 Mar 2. PMID:17337440<ref>PMID:17337440</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ol2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17337440}}, adds the Publication Abstract to the page
+*[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17337440 is the PubMed ID number.
+*[[Serpin 3D structures|Serpin 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_17337440}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-[[2ol2]] is a 2 chain structure 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=2OL2 OCA].
-==Reference==
-<ref group="xtra">PMID:17337440</ref><ref group="xtra">PMID:12575940</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Huntington, J A.]]
+[[Category: Large Structures]]
-[[Category: Li, W.]]
+[[Category: Huntington JA]]
-[[Category: Hydrolase inhibitor]]
+[[Category: Li W]]
-[[Category: Serpin]]