6f3v: Difference between revisions
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==Backbone structure of bradykinin (BK) peptide bound to human Bradykinin 2 Receptor (B2R) determined by MAS SSNMR== | ==Backbone structure of bradykinin (BK) peptide bound to human Bradykinin 2 Receptor (B2R) determined by MAS SSNMR== | ||
<StructureSection load='6f3v' size='340' side='right'caption='[[6f3v | <StructureSection load='6f3v' size='340' side='right'caption='[[6f3v]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f3v]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3V OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6f3v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3V FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=6f3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3v OCA], [https://pdbe.org/6f3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3v RCSB], [https://www.ebi.ac.uk/pdbsum/6f3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== 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 == | |||
[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 == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Glaubitz | [[Category: Glaubitz C]] | ||
[[Category: Kuenze | [[Category: Kuenze G]] | ||
[[Category: Lopez | [[Category: Lopez JJ]] | ||
[[Category: Mao | [[Category: Mao J]] | ||
[[Category: Meiler | [[Category: Meiler J]] | ||
[[Category: Michel | [[Category: Michel H]] | ||
[[Category: Schwalbe | [[Category: Schwalbe H]] | ||
[[Category: Shukla | [[Category: Shukla AK]] | ||