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| | <StructureSection load='1hcf' size='340' side='right'caption='[[1hcf]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1hcf' size='340' side='right'caption='[[1hcf]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hcf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hcf]] is a 4 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=1HCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wwb|1wwb]], [[1b8m|1b8m]], [[1b98|1b98]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1hcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcf OCA], [https://pdbe.org/1hcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcf RCSB], [https://www.ebi.ac.uk/pdbsum/1hcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcf 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=1hcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcf OCA], [https://pdbe.org/1hcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcf RCSB], [https://www.ebi.ac.uk/pdbsum/1hcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/NTF4_HUMAN NTF4_HUMAN]] Defects in NTF4 may be associated with susceptibility to primary open angle glaucoma type 1O (GLC1O) [MIM:[https://omim.org/entry/613100 613100]]. A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. The disease is asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
| + | [https://www.uniprot.org/uniprot/NTF4_HUMAN NTF4_HUMAN] Defects in NTF4 may be associated with susceptibility to primary open angle glaucoma type 1O (GLC1O) [MIM:[https://omim.org/entry/613100 613100]. A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. The disease is asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NTF4_HUMAN NTF4_HUMAN]] Target-derived survival factor for peripheral sensory sympathetic neurons.
| + | [https://www.uniprot.org/uniprot/NTF4_HUMAN NTF4_HUMAN] Target-derived survival factor for peripheral sensory sympathetic neurons. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allen, S J]] | + | [[Category: Allen SJ]] |
| - | [[Category: Banfield, M J]] | + | [[Category: Banfield MJ]] |
| - | [[Category: Brady, R L]] | + | [[Category: Brady RL]] |
| - | [[Category: Dawbarn, D]] | + | [[Category: Dawbarn D]] |
| - | [[Category: Naylor, R L]] | + | [[Category: Naylor RL]] |
| - | [[Category: Robertson, A G.S]] | + | [[Category: Robertson AGS]] |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Neurotrophin-4/5]]
| + | |
| - | [[Category: Ngf-beta superfamily]]
| + | |
| - | [[Category: Transferase-hormone complex]]
| + | |
| - | [[Category: Transferase/hormone]]
| + | |
| - | [[Category: Trkb receptor]]
| + | |
| Structural highlights
Disease
NTF4_HUMAN Defects in NTF4 may be associated with susceptibility to primary open angle glaucoma type 1O (GLC1O) [MIM:613100. A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. The disease is asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
Function
NTF4_HUMAN Target-derived survival factor for peripheral sensory sympathetic 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
BACKGROUND: The binding of neurotrophin ligands to their respective Trk cellular receptors initiates intracellular signals essential for the growth and survival of neurons. The site of neurotrophin binding has been located to the fifth extracellular domain of the Trk receptor, with this region regulating both the affinity and specificity of Trk receptor:neurotrophin interaction. Neurotrophin function has been implicated in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease. RESULTS: We have determined the 2.7 A crystal structure of neurotrophin-4/5 bound to the neurotrophin binding domain of its high-affinity receptor TrkB (TrkB-d5). As previously seen in the interaction of nerve growth factor with TrkA, neurotrophin-4/5 forms a crosslink between two spatially distant receptor molecules. The contacts formed in the TrkB-d5:neurotrophin-4/5 complex can be divided into a conserved area similar to a region observed in the TrkA-d5:NGF complex and a second site-unique in each ligand-receptor pair-formed primarily by the ordering of the neurotrophin N terminus. CONCLUSIONS: Together, the structures of the TrkB-d5:NT-4/5 and TrkA-d5:NGF complexes confirm a consistent pattern of recognition in Trk receptor:neurotrophin complex formation. In both cases, the N terminus of the neurotrophin becomes ordered only on complex formation. This ordering appears to be directed largely by the receptor surface, with the resulting complementary surfaces providing the main determinant of receptor specificity. These features provide an explanation both for the limited crossreactivity observed between the range of neurotrophins and Trk receptors and for the high-affinity binding associated with respective ligand-receptor pairs.
Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5.,Banfield MJ, Naylor RL, Robertson AG, Allen SJ, Dawbarn D, Brady RL Structure. 2001 Dec;9(12):1191-9. PMID:11738045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Banfield MJ, Naylor RL, Robertson AG, Allen SJ, Dawbarn D, Brady RL. Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5. Structure. 2001 Dec;9(12):1191-9. PMID:11738045
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