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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[3buk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BUK FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3buk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BUK FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nt3|1nt3]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NT-3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Ngfr, Tnfrsf16 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3buk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3buk OCA], [https://pdbe.org/3buk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3buk RCSB], [https://www.ebi.ac.uk/pdbsum/3buk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3buk 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=3buk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3buk OCA], [https://pdbe.org/3buk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3buk RCSB], [https://www.ebi.ac.uk/pdbsum/3buk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3buk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NTF3_HUMAN NTF3_HUMAN]] Seems to promote the survival of visceral and proprioceptive sensory neurons. [[https://www.uniprot.org/uniprot/TNR16_RAT TNR16_RAT]] Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells.
| + | [https://www.uniprot.org/uniprot/NTF3_HUMAN NTF3_HUMAN] Seems to promote the survival of visceral and proprioceptive sensory neurons. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| - | [[Category: Cao, P]] | + | [[Category: Cao P]] |
| - | [[Category: Gong, Y]] | + | [[Category: Gong Y]] |
| - | [[Category: Jiang, T]] | + | [[Category: Jiang T]] |
| - | [[Category: Yu, H J]] | + | [[Category: Yu HJ]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Beta-sheet]]
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| - | [[Category: Cleavage on pair of basic residue]]
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| - | [[Category: Developmental protein]]
| + | |
| - | [[Category: Differentiation]]
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| - | [[Category: Glycoprotein]]
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| - | [[Category: Growth factor]]
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| - | [[Category: Ligand-receptor complex]]
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| - | [[Category: Membrane]]
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| - | [[Category: Neurogenesis]]
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| - | [[Category: Neurotrophin-3]]
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| - | [[Category: P75ntr]]
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| - | [[Category: Secreted]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: Transmembrane]]
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| Structural highlights
Function
NTF3_HUMAN Seems to promote the survival of visceral and proprioceptive sensory neurons.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Neurotrophins (NTs) are important regulators for the survival, differentiation and maintenance of different peripheral and central neurons. NTs bind to two distinct classes of glycosylated receptor: the p75 neurotrophin receptor (p75(NTR)) and tyrosine kinase receptors (Trks). Whereas p75(NTR) binds to all NTs, the Trk subtypes are specific for each NT. The question of whether NTs stimulate p75(NTR) by inducing receptor homodimerization is still under debate. Here we report the 2.6-A resolution crystal structure of neurotrophin-3 (NT-3) complexed to the ectodomain of glycosylated p75(NTR). In contrast to the previously reported asymmetric complex structure, which contains a dimer of nerve growth factor (NGF) bound to a single ectodomain of deglycosylated p75(NTR) (ref. 3), we show that NT-3 forms a central homodimer around which two glycosylated p75(NTR) molecules bind symmetrically. Symmetrical binding occurs along the NT-3 interfaces, resulting in a 2:2 ligand-receptor cluster. A comparison of the symmetrical and asymmetric structures reveals significant differences in ligand-receptor interactions and p75(NTR) conformations. Biochemical experiments indicate that both NT-3 and NGF bind to p75(NTR) with 2:2 stoichiometry in solution, whereas the 2:1 complexes are the result of artificial deglycosylation. We therefore propose that the symmetrical 2:2 complex reflects a native state of p75(NTR) activation at the cell surface. These results provide a model for NTs-p75(NTR) recognition and signal generation, as well as insights into coordination between p75(NTR) and Trks.
Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex.,Gong Y, Cao P, Yu HJ, Jiang T Nature. 2008 Aug 7;454(7205):789-93. Epub 2008 Jul 2. PMID:18596692[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gong Y, Cao P, Yu HJ, Jiang T. Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex. Nature. 2008 Aug 7;454(7205):789-93. Epub 2008 Jul 2. PMID:18596692 doi:10.1038/nature07089
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