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1SG1

Crystal Structure of the Receptor-Ligand Complex between Nerve Growth Factor and the Common Neurotrophin Receptor p75

Summary for 1SG1
Entry DOI10.2210/pdb1sg1/pdb
DescriptorBeta-nerve growth factor, Tumor necrosis factor receptor superfamily member 16, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsnerve 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 sourceHomo sapiens (human)
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Cellular locationSecreted: P01138
Membrane; Single-pass type I membrane protein: P07174
Total number of polymer chains3
Total formula weight44324.29
Authors
He, X.L.,Garcia, K.C. (deposition date: 2004-02-22, release date: 2004-06-01, Last modification date: 2023-08-23)
Primary citationHe, 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: 15131306
DOI: 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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数据于2024-10-30公开中

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