1hcf
From Proteopedia
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- | [[Image:1hcf.jpg|left|200px]] | + | [[Image:1hcf.jpg|left|200px]] |
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- | '''CRYSTAL STRUCTURE OF TRKB-D5 BOUND TO NEUROTROPHIN-4/5''' | + | {{Structure |
+ | |PDB= 1hcf |SIZE=350|CAPTION= <scene name='initialview01'>1hcf</scene>, resolution 2.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF TRKB-D5 BOUND TO NEUROTROPHIN-4/5''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1HCF is a [ | + | 1HCF is a [[Protein complex]] structure of sequences from [http://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]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11738045 11738045] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: trkb receptor]] | [[Category: trkb receptor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:20 2008'' |
Revision as of 09:35, 20 March 2008
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, resolution 2.7Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF TRKB-D5 BOUND TO NEUROTROPHIN-4/5
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Obesity, hyperphagia, and developmental delay OMIM:[600456]
About this Structure
1HCF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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