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TitleRET recognition of GDNF-GFRα1 ligand by a composite binding site promotes membrane-proximal self-association.
Journal, issue, pagesCell Rep, Vol. 8, Issue 6, Page 1894-1904, Year 2014
Publish dateSep 25, 2014
AuthorsKerry M Goodman / Svend Kjær / Fabienne Beuron / Phillip P Knowles / Agata Nawrotek / Emily M Burns / Andrew G Purkiss / Roger George / Massimo Santoro / Edward P Morris / Neil Q McDonald /
PubMed AbstractThe RET receptor tyrosine kinase is essential to vertebrate development and implicated in multiple human diseases. RET binds a cell surface bipartite ligand comprising a GDNF family ligand and a ...The RET receptor tyrosine kinase is essential to vertebrate development and implicated in multiple human diseases. RET binds a cell surface bipartite ligand comprising a GDNF family ligand and a GFRα coreceptor, resulting in RET transmembrane signaling. We present a hybrid structural model, derived from electron microscopy (EM) and low-angle X-ray scattering (SAXS) data, of the RET extracellular domain (RET(ECD)), GDNF, and GFRα1 ternary complex, defining the basis for ligand recognition. RET(ECD) envelopes the dimeric ligand complex through a composite binding site comprising four discrete contact sites. The GFRα1-mediated contacts are crucial, particularly close to the invariant RET calcium-binding site, whereas few direct contacts are made by GDNF, explaining how distinct ligand/coreceptor pairs are accommodated. The RET(ECD) cysteine-rich domain (CRD) contacts both ligand components and makes homotypic membrane-proximal interactions occluding three different antibody epitopes. Coupling of these CRD-mediated interactions suggests models for ligand-induced RET activation and ligand-independent oncogenic deregulation.
External linksCell Rep / PubMed:25242331
MethodsEM (single particle)
Resolution24.0 - 26.0 Å
Structure data

2712

4ux8

EMDB-2712: Structure of the RET receptor tyrosine kinase extracellular domain
PDB-4ux8: RET recognition of GDNF-GFRalpha1 ligand by a composite binding site promotes membrane-proximal self-association
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-2713:
Structure of the zebrafish RET tyrosine kinase extracellular domain
Method: EM (single particle) / Resolution: 26.0 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
  • Danio rerio (zebrafish)
KeywordsSIGNALING PROTEIN / VERTEBRATE DEVELOPMENT / HUMAN DISEASES / PART OF THE RET-GFL- GFRA COMPLEX

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