6a8o: Difference between revisions
New page: '''Unreleased structure''' The entry 6a8o is ON HOLD Authors: Xu, M., Jiang, L., Huang, M. Description: Crystal structures of the serine protease domain of murine plasma kallikrein [[C... |
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The | ==Crystal structures of the serine protease domain of murine plasma kallikrein with peptide inhibitor mupain-1-16== | ||
<StructureSection load='6a8o' size='340' side='right'caption='[[6a8o]], [[Resolution|resolution]] 2.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a8o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthemiopsis Synthemiopsis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A8O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MRZ:PIPERIDINE-1-CARBOXIMIDAMIDE'>MRZ</scene></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=6a8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8o OCA], [https://pdbe.org/6a8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a8o RCSB], [https://www.ebi.ac.uk/pdbsum/6a8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KLKB1_MOUSE KLKB1_MOUSE] The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serine proteases play important roles in numerous physiological and pathophysiological processes. Moreover, serine proteases are classical subjects for studies of catalytic and inhibitory mechanisms of enzymes. Here, we determined the crystal structures of a serine protease, murine plasma kallikrein (mPK), and its complex with a peptidic inhibitor. Although mPK in the complex adopts a canonical protease structure, the apo-mPK exhibits a previously unobserved structural feature: the entrance of the intact S1 pocket is blocked by Glu217. In addition, molecular dynamics simulations and functional assays support the flexibility of Glu217 and suggest that this flexibility plays a role in regulating the activity of serine proteases. ENZYMES: EC: 3.4.21.34. | |||
Crystal structure of plasma kallikrein reveals the unusual flexibility of the S1 pocket triggered by Glu217.,Xu M, Chen Y, Xu P, Andreasen PA, Jiang L, Li J, Huang M FEBS Lett. 2018 Aug;592(15):2658-2667. doi: 10.1002/1873-3468.13191. Epub 2018, Jul 30. PMID:30019481<ref>PMID:30019481</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Huang | <div class="pdbe-citations 6a8o" style="background-color:#fffaf0;"></div> | ||
[[Category: Jiang | |||
[[Category: Xu | ==See Also== | ||
*[[Kallikrein 3D structures|Kallikrein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Synthemiopsis]] | |||
[[Category: Huang M]] | |||
[[Category: Jiang L]] | |||
[[Category: Xu M]] | |||
Latest revision as of 12:21, 22 November 2023
Crystal structures of the serine protease domain of murine plasma kallikrein with peptide inhibitor mupain-1-16Crystal structures of the serine protease domain of murine plasma kallikrein with peptide inhibitor mupain-1-16
Structural highlights
FunctionKLKB1_MOUSE The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. Publication Abstract from PubMedSerine proteases play important roles in numerous physiological and pathophysiological processes. Moreover, serine proteases are classical subjects for studies of catalytic and inhibitory mechanisms of enzymes. Here, we determined the crystal structures of a serine protease, murine plasma kallikrein (mPK), and its complex with a peptidic inhibitor. Although mPK in the complex adopts a canonical protease structure, the apo-mPK exhibits a previously unobserved structural feature: the entrance of the intact S1 pocket is blocked by Glu217. In addition, molecular dynamics simulations and functional assays support the flexibility of Glu217 and suggest that this flexibility plays a role in regulating the activity of serine proteases. ENZYMES: EC: 3.4.21.34. Crystal structure of plasma kallikrein reveals the unusual flexibility of the S1 pocket triggered by Glu217.,Xu M, Chen Y, Xu P, Andreasen PA, Jiang L, Li J, Huang M FEBS Lett. 2018 Aug;592(15):2658-2667. doi: 10.1002/1873-3468.13191. Epub 2018, Jul 30. PMID:30019481[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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