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| <StructureSection load='6a8o' size='340' side='right'caption='[[6a8o]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='6a8o' size='340' side='right'caption='[[6a8o]], [[Resolution|resolution]] 2.77Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6a8o]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8O FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MRZ:PIPERIDINE-1-CARBOXIMIDAMIDE'>MRZ</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klkb1, Klk3, Pk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Plasma_kallikrein Plasma kallikrein], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.34 3.4.21.34] </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=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> |
- | <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=6a8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8o OCA], [http://pdbe.org/6a8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8o RCSB], [http://www.ebi.ac.uk/pdbsum/6a8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8o ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Plasma kallikrein]]
| + | |
| [[Category: Synthemiopsis]] | | [[Category: Synthemiopsis]] |
- | [[Category: Huang, M]] | + | [[Category: Huang M]] |
- | [[Category: Jiang, L]] | + | [[Category: Jiang L]] |
- | [[Category: Xu, M]] | + | [[Category: Xu M]] |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Murine plasma kallikrein]]
| + | |
- | [[Category: Serine protease]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xu M, Chen Y, Xu P, Andreasen PA, Jiang L, Li J, Huang M. Crystal structure of plasma kallikrein reveals the unusual flexibility of the S1 pocket triggered by Glu217. FEBS Lett. 2018 Aug;592(15):2658-2667. doi: 10.1002/1873-3468.13191. Epub 2018, Jul 30. PMID:30019481 doi:http://dx.doi.org/10.1002/1873-3468.13191
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