|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5f03' size='340' side='right'caption='[[5f03]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='5f03' size='340' side='right'caption='[[5f03]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F03 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f03]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F03 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5TA:(5~{S})-5-[[3-(AMINOMETHYL)PHENOXY]METHYL]-3-[3-[2-(2-CHLORANYLPYRIDIN-3-YL)ETHYNYL]PHENYL]-1,3-OXAZOLIDIN-2-ONE'>5TA</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]] 1.94Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPSB2, TPS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5TA:(5~{S})-5-[[3-(AMINOMETHYL)PHENOXY]METHYL]-3-[3-[2-(2-CHLORANYLPYRIDIN-3-YL)ETHYNYL]PHENYL]-1,3-OXAZOLIDIN-2-ONE'>5TA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] </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=5f03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f03 OCA], [https://pdbe.org/5f03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f03 RCSB], [https://www.ebi.ac.uk/pdbsum/5f03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f03 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=5f03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f03 OCA], [http://pdbe.org/5f03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f03 RCSB], [http://www.ebi.ac.uk/pdbsum/5f03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f03 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRYB2_HUMAN TRYB2_HUMAN]] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection (By similarity). | + | [https://www.uniprot.org/uniprot/TRYB1_HUMAN TRYB1_HUMAN] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tryptase]]
| + | [[Category: Banner D]] |
| - | [[Category: Banner, D]] | + | [[Category: Benz J]] |
| - | [[Category: Benz, J]] | + | [[Category: Joseph C]] |
| - | [[Category: Joseph, C]] | + | [[Category: Kuglstatter A]] |
| - | [[Category: Kuglstatter, A]] | + | |
| - | [[Category: Human tryptase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine proteinase]]
| + | |
| Structural highlights
Function
TRYB1_HUMAN Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type (By similarity).
Publication Abstract from PubMed
We present a series of small molecule drug discovery case studies where computational methods were prospectively employed to impact Roche research projects, with the aim of highlighting those methods that provide real added value. Our brief accounts encompass a broad range of methods and techniques applied to a variety of enzymes and receptors. Most of these are based on judicious application of knowledge about molecular conformations and interactions: filling of lipophilic pockets to gain affinity or selectivity, addition of polar substituents, scaffold hopping, transfer of SAR, conformation analysis, and molecular overlays. A case study of sequence-driven focused screening is presented to illustrate how appropriate preprocessing of information enables effective exploitation of prior knowledge. We conclude that qualitative statements enabling chemists to focus on promising regions of chemical space are often more impactful than quantitative prediction.
A Real-World Perspective on Molecular Design.,Kuhn B, Guba W, Hert J, Banner D, Bissantz C, Ceccarelli S, Haap W, Korner M, Kuglstatter A, Lerner C, Mattei P, Neidhart W, Pinard E, Rudolph MG, Schulz-Gasch T, Woltering T, Stahl M J Med Chem. 2016 Feb 24. PMID:26878596[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuhn B, Guba W, Hert J, Banner D, Bissantz C, Ceccarelli S, Haap W, Korner M, Kuglstatter A, Lerner C, Mattei P, Neidhart W, Pinard E, Rudolph MG, Schulz-Gasch T, Woltering T, Stahl M. A Real-World Perspective on Molecular Design. J Med Chem. 2016 Feb 24. PMID:26878596 doi:http://dx.doi.org/10.1021/acs.jmedchem.5b01875
|
