6f3y
From Proteopedia
(Difference between revisions)
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<StructureSection load='6f3y' size='340' side='right'caption='[[6f3y]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='6f3y' size='340' side='right'caption='[[6f3y]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6f3y]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3Y OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6f3y]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3Y FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f3x|6f3x]], [[6f3w|6f3w]], [[6f3v|6f3v]], [[6f27|6f27]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6f3x|6f3x]], [[6f3w|6f3w]], [[6f3v|6f3v]], [[6f27|6f27]]</div></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=6f3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3y OCA], [https://pdbe.org/6f3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3y RCSB], [https://www.ebi.ac.uk/pdbsum/6f3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3y ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/KNG1_HUMAN KNG1_HUMAN]] Congenital high-molecular-weight kininogen deficiency. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/KNG1_HUMAN KNG1_HUMAN]] (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 07:40, 25 June 2021
Backbone structure of Des-Arg10-Kallidin (DAKD) peptide bound to human Bradykinin 1 Receptor (B1R) determined by DNP-enhanced MAS SSNMR
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Categories: Large Structures | Glaubitz, C | Joedicke, L | Kuenze, G | Mao, J | Meiler, J | Michel, H | Dnp | Gpcr | Membrane protein