|
|
(2 intermediate revisions not shown.) |
Line 1: |
Line 1: |
| + | |
| ==Structural basis of neurohormone perception by the receptor tyrosine kinase Torso== | | ==Structural basis of neurohormone perception by the receptor tyrosine kinase Torso== |
- | <StructureSection load='5aoq' size='340' side='right' caption='[[5aoq]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='5aoq' size='340' side='right'caption='[[5aoq]], [[Resolution|resolution]] 2.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5aoq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AOQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5aoq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AOQ FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </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=5aoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aoq OCA], [https://pdbe.org/5aoq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aoq RCSB], [https://www.ebi.ac.uk/pdbsum/5aoq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aoq 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=5aoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aoq OCA], [http://pdbe.org/5aoq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aoq RCSB], [http://www.ebi.ac.uk/pdbsum/5aoq PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/TORSO_BOMMO TORSO_BOMMO] Probable receptor tyrosine kinase. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone (PTTH) (By similarity). Binding to PTTH stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (PubMed:19965758, PubMed:26928300).[UniProtKB:P18475]<ref>PMID:19965758</ref> <ref>PMID:26928300</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
Line 20: |
Line 22: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Receptor protein-tyrosine kinase]] | + | [[Category: Bombyx mori]] |
- | [[Category: Goyal, Y]] | + | [[Category: Large Structures]] |
- | [[Category: Grotthuss, M von]] | + | [[Category: Goyal Y]] |
- | [[Category: Jenni, S]] | + | [[Category: Jenni S]] |
- | [[Category: Klein, D E]] | + | [[Category: Klein DE]] |
- | [[Category: Shvartsman, S Y]] | + | [[Category: Shvartsman SY]] |
- | [[Category: Cystine knot]] | + | [[Category: Von Grotthuss M]] |
- | [[Category: Developmental timing]]
| + | |
- | [[Category: Fibronectin type iii domain]]
| + | |
- | [[Category: Metamorphosis]]
| + | |
- | [[Category: Negative cooperativity]]
| + | |
- | [[Category: Neurohormone]]
| + | |
- | [[Category: Peptide hormone]]
| + | |
- | [[Category: Prothoracicotropic hormone]]
| + | |
- | [[Category: Ptth]]
| + | |
- | [[Category: Receptor tyrosine kinase]]
| + | |
- | [[Category: Rtk]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TORSO_BOMMO Probable receptor tyrosine kinase. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone (PTTH) (By similarity). Binding to PTTH stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (PubMed:19965758, PubMed:26928300).[UniProtKB:P18475][1] [2]
Publication Abstract from PubMed
In insects, brain-derived Prothoracicotropic hormone (PTTH) activates the receptor tyrosine kinase (RTK) Torso to initiate metamorphosis through the release of ecdysone. We have determined the crystal structure of silkworm PTTH in complex with the ligand-binding region of Torso. Here we show that ligand-induced Torso dimerization results from the sequential and negatively cooperative formation of asymmetric heterotetramers. Mathematical modeling of receptor activation based upon our biophysical studies shows that ligand pulses are "buffered" at low receptor levels, leading to a sustained signal. By contrast, high levels of Torso develop the signal intensity and duration of a noncooperative system. We propose that this may allow Torso to coordinate widely different functions from a single ligand by tuning receptor levels. Phylogenic analysis indicates that Torso is found outside arthropods, including human parasitic roundworms. Together, our findings provide mechanistic insight into how this receptor system, with roles in embryonic and adult development, is regulated.
Structural Basis of Neurohormone Perception by the Receptor Tyrosine Kinase Torso.,Jenni S, Goyal Y, von Grotthuss M, Shvartsman SY, Klein DE Mol Cell. 2015 Dec 17;60(6):941-52. doi: 10.1016/j.molcel.2015.10.026. Epub 2015 , Nov 19. PMID:26698662[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rewitz KF, Yamanaka N, Gilbert LI, O'Connor MB. The insect neuropeptide PTTH activates receptor tyrosine kinase torso to initiate metamorphosis. Science. 2009 Dec 4;326(5958):1403-5. PMID:19965758 doi:10.1126/science.1176450
- ↑ Konogami T, Yang Y, Ogihara MH, Hikiba J, Kataoka H, Saito K. Ligand-dependent responses of the silkworm prothoracicotropic hormone receptor, Torso, are maintained by unusual intermolecular disulfide bridges in the transmembrane region. Sci Rep. 2016 Mar 1;6:22437. PMID:26928300 doi:10.1038/srep22437
- ↑ Jenni S, Goyal Y, von Grotthuss M, Shvartsman SY, Klein DE. Structural Basis of Neurohormone Perception by the Receptor Tyrosine Kinase Torso. Mol Cell. 2015 Dec 17;60(6):941-52. doi: 10.1016/j.molcel.2015.10.026. Epub 2015 , Nov 19. PMID:26698662 doi:http://dx.doi.org/10.1016/j.molcel.2015.10.026
|