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| {{STRUCTURE_2ifg| PDB=2ifg | SCENE= }} | | {{STRUCTURE_2ifg| PDB=2ifg | SCENE= }} |
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| '''Structure of the extracellular segment of human TRKA in complex with nerve growth factor'''
| | ===Structure of the extracellular segment of human TRKA in complex with nerve growth factor=== |
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| ==Overview==
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| Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and p75, which have been proposed to create a "high-affinity" NGF binding site through formation of a ternary TrkA/NGF/p75 complex. To define a structural basis for the high-affinity site, we have determined the three-dimensional structure of a complete extracellular domain of TrkA complexed with NGF. The complex reveals a crab-shaped homodimeric TrkA structure, but a mechanism for p75 coordination is not obvious. We investigated the heterodimerization of membrane-bound TrkA and p75, on intact mammalian cells, using a beta-gal protein-protein interaction system. We find that NGF dimerizes TrkA and that p75 exists on the cell surface as a preformed oligomer that is not dissociated by NGF. We find no evidence for a direct TrkA/p75 interaction. We propose that TrkA and p75 likely communicate through convergence of downstream signaling pathways and/or shared adaptor molecules, rather than through direct extracellular interactions.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17196528}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17196528 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17196528}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Trk]] | | [[Category: Trk]] |
| [[Category: Trka]] | | [[Category: Trka]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:26:44 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:27:18 2008'' |
