6f3w: Difference between revisions

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==Backbone structure of free bradykinin (BK) in DDM/CHS detergent micelle determined by MAS SSNMR==
==Backbone structure of free bradykinin (BK) in DDM/CHS detergent micelle determined by MAS SSNMR==
<StructureSection load='6f3w' size='340' side='right' caption='[[6f3w]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='6f3w' size='340' side='right'caption='[[6f3w]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6f3w]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F3W FirstGlance]. <br>
<table><tr><td colspan='2'>[[6f3w]] 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=6F3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3W FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f3v|6f3v]], [[6f27|6f27]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3w OCA], [http://pdbe.org/6f3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f3w RCSB], [http://www.ebi.ac.uk/pdbsum/6f3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3w ProSAT]</span></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=6f3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3w OCA], [https://pdbe.org/6f3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3w RCSB], [https://www.ebi.ac.uk/pdbsum/6f3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3w ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://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.  
[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 ==
[[http://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.  
[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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glaubitz, C]]
[[Category: Homo sapiens]]
[[Category: Kuenze, G]]
[[Category: Large Structures]]
[[Category: Lopez, J J]]
[[Category: Glaubitz C]]
[[Category: Mao, J]]
[[Category: Kuenze G]]
[[Category: Meiler, J]]
[[Category: Lopez JJ]]
[[Category: Michel, H]]
[[Category: Mao J]]
[[Category: Schwalbe, H]]
[[Category: Meiler J]]
[[Category: Shukla, A K]]
[[Category: Michel H]]
[[Category: Dnp]]
[[Category: Schwalbe H]]
[[Category: Gpcr]]
[[Category: Shukla AK]]
[[Category: Membrane protein]]

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