X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding
- 1 June 1997
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (6) , 435-438
- https://doi.org/10.1038/nsb0697-435
Abstract
The crystal structure of glial cell-derived neurotrophic factor (GDNF) reveals two independent copies of the dimer that differ significantly through a hinge bending at the central, disulphide-rich region. GDNF is compared with other members of the TGF-β family, and potential receptor binding surfaces are identified.Keywords
This publication has 17 references indexed in Scilit:
- Characterization of a multicomponent receptor for GDNFNature, 1996
- GDNF–Induced Activation of the Ret Protein Tyrosine Kinase Is Mediated by GDNFR-α, a Novel Receptor for GDNFCell, 1996
- Functional recovery in parkinsonian monkeys treated with GDNFNature, 1996
- Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.Proceedings of the National Academy of Sciences, 1996
- Mechanism of Activation of the ret Proto-oncogene by Multiple Endocrine Neoplasia 2A MutationsMolecular and Cellular Biology, 1995
- GDNF: a Glial Cell Line-Derived Neurotrophic Factor for Midbrain Dopaminergic NeuronsScience, 1993
- Variability of conformations at crystal contacts in BPTI represent true low‐energy structures: Correspondence among lattice packing and molecular dynamics structuresProteins-Structure Function and Bioinformatics, 1992
- Crystal Structure of Transforming Growth Factor-β2: an Unusual Fold for the SuperfamilyScience, 1992
- An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth fact or-β2Nature, 1992
- New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factorNature, 1991