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| | <StructureSection load='6h8m' size='340' side='right'caption='[[6h8m]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6h8m' size='340' side='right'caption='[[6h8m]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6h8m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H8M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6h8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H8M FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prss12, Bssp3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 1.7Å</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=6h8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h8m OCA], [http://pdbe.org/6h8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h8m RCSB], [http://www.ebi.ac.uk/pdbsum/6h8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h8m 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=6h8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h8m OCA], [https://pdbe.org/6h8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h8m RCSB], [https://www.ebi.ac.uk/pdbsum/6h8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h8m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/NETR_MOUSE NETR_MOUSE]] Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. | |
| | <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: Canciani, A]] | + | [[Category: Canciani A]] |
| - | [[Category: Forneris, F]] | + | [[Category: Forneris F]] |
| - | [[Category: Crd domain]]
| + | |
| - | [[Category: Extracellular protease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Neurotrypsin]]
| + | |
| - | [[Category: Srcr domain]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Neurotrypsin (NT) is a multi-domain serine protease of the nervous system with only one known substrate: the large proteoglycan Agrin. NT has seen to be involved in the maintenance/turnover of neuromuscular junctions and in processes of synaptic plasticity in the central nervous system. Roles which have been tied to its enzymatic activity, localized in the C-terminal serine-protease (SP) domain. However the purpose of NT's remaining 3-4 scavenger receptor cysteine-rich (SRCR) domains is still unclear. We have determined the crystal structure of the third SRCR domain of murine NT (mmNT-SRCR3), immediately preceding the SP domain and performed a comparative structural analysis using homologous SRCR structures. Our data and the elevated degree of structural conservation with homologous domains highlight possible functional roles for NT SRCRs. Computational and experimental analyses suggest the identification of a putative binding region for Ca(2+) ions, known to regulate NT enzymatic activity. Furthermore, sequence and structure comparisons allow to single out regions of interest that, in future studies, might be implicated in Agrin recognition/binding or in interactions with as of yet undiscovered NT partners. This article is protected by copyright. All rights reserved.
Structural characterization of the third scavenger receptor cysteine-rich domain of murine Neurotrypsin.,Canciani A, Catucci G, Forneris F Protein Sci. 2019 Feb 12. doi: 10.1002/pro.3587. PMID:30748049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Canciani A, Catucci G, Forneris F. Structural characterization of the third scavenger receptor cysteine-rich domain of murine Neurotrypsin. Protein Sci. 2019 Feb 12. doi: 10.1002/pro.3587. PMID:30748049 doi:http://dx.doi.org/10.1002/pro.3587
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