2hi9
From Proteopedia
(Difference between revisions)
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==Crystal Structure of human native protein C inhibitor== | ==Crystal Structure of human native protein C inhibitor== | ||
- | <StructureSection load='2hi9' size='340' side='right' caption='[[2hi9]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2hi9' size='340' side='right'caption='[[2hi9]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2hi9]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2hi9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HI9 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lq8|1lq8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lq8|1lq8]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINA5 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINA5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi9 OCA], [https://pdbe.org/2hi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hi9 RCSB], [https://www.ebi.ac.uk/pdbsum/2hi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hi9 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Adams, T E]] | [[Category: Adams, T E]] | ||
[[Category: Huntington, J A]] | [[Category: Huntington, J A]] |
Revision as of 07:40, 17 March 2021
Crystal Structure of human native protein C inhibitor
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