2GYR
Crystal structure of human artemin
Summary for 2GYR
| Entry DOI | 10.2210/pdb2gyr/pdb |
| Descriptor | Neurotrophic factor artemin, isoform 3 (1 entity in total) |
| Functional Keywords | neurotrophic factor, cystein-knot, hormone-growth factor complex, hormone/growth factor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted (By similarity): Q5T4W7 |
| Total number of polymer chains | 6 |
| Total formula weight | 69445.79 |
| Authors | Wang, X.Q. (deposition date: 2006-05-09, release date: 2006-06-27, Last modification date: 2024-10-30) |
| Primary citation | Wang, X.,Baloh, R.H.,Milbrandt, J.,Garcia, K.C. Structure of Artemin Complexed with Its Receptor GFRalpha3: Convergent Recognition of Glial Cell Line-Derived Neurotrophic Factors. Structure, 14:1083-1092, 2006 Cited by PubMed Abstract: Artemin (ARTN) is a member of the glial cell line-derived neurotrophic factor (GDNF) family ligands (GFLs) which regulate the development and maintenance of many neuronal populations in the mammalian nervous system. Here we report the 1.92 A crystal structure of the complex formed between ARTN and its receptor GFRalpha3, which is the initiating step in the formation of a ternary signaling complex containing the shared RET receptor. It represents a new receptor-ligand interaction mode for the TGF-beta superfamily that reveals both conserved and specificity-determining anchor points for all GFL-GFRalpha pairs. In tandem with the complex structure, cellular studies using receptor chimeras implicate dyad-symmetric composite interfaces for recruitment and dimerization of RET, leading to intracellular signaling. These studies should facilitate the functional dissection of the specific versus pleiotropic roles of this system in neurobiology, as well as its exploitation for therapeutic applications. PubMed: 16765900DOI: 10.1016/j.str.2006.05.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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