1SG1
Crystal Structure of the Receptor-Ligand Complex between Nerve Growth Factor and the Common Neurotrophin Receptor p75
Summary for 1SG1
Entry DOI | 10.2210/pdb1sg1/pdb |
Descriptor | Beta-nerve growth factor, Tumor necrosis factor receptor superfamily member 16, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | nerve growth factor, ngf, p75, neurotrophin, common neurotrophin receptor, growth factor receptor, receptor-ligand complex, hormone-growth factor-membrane protein complex, hormone/growth factor/membrane protein |
Biological source | Homo sapiens (human) More |
Cellular location | Secreted: P01138 Membrane; Single-pass type I membrane protein: P07174 |
Total number of polymer chains | 3 |
Total formula weight | 44324.29 |
Authors | He, X.L.,Garcia, K.C. (deposition date: 2004-02-22, release date: 2004-06-01, Last modification date: 2023-08-23) |
Primary citation | He, X.L.,Garcia, K.C. Structure of nerve growth factor complexed with the shared neurotrophin receptor p75 Science, 304:870-875, 2004 Cited by PubMed Abstract: Neurotrophins are secreted growth factors critical for the development and maintenance of the vertebrate nervous system. Neurotrophins activate two types of cell surface receptors, the Trk receptor tyrosine kinases and the shared p75 neurotrophin receptor. We have determined the 2.4 A crystal structure of the prototypic neurotrophin, nerve growth factor (NGF), complexed with the extracellular domain of p75. Surprisingly, the complex is composed of an NGF homodimer asymmetrically bound to a single p75. p75 binds along the homodimeric interface of NGF, which disables NGF's symmetry-related second p75 binding site through an allosteric conformational change. Thus, neurotrophin signaling through p75 may occur by disassembly of p75 dimers and assembly of asymmetric 2:1 neurotrophin/p75 complexes, which could potentially engage a Trk receptor to form a trimolecular signaling complex. PubMed: 15131306DOI: 10.1126/science.1095190 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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