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| {{STRUCTURE_1q8d| PDB=1q8d | SCENE= }} | | {{STRUCTURE_1q8d| PDB=1q8d | SCENE= }} |
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| '''The crystal structure of GDNF family co-receptor alpha 1 domain 3'''
| | ===The crystal structure of GDNF family co-receptor alpha 1 domain 3=== |
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| ==Overview==
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| Glial cell line-derived neurotrophic factor (GDNF) binds to the GDNF family co-receptor alpha1 (GFRalpha1) and activates RET receptor tyrosine kinase. GFRalpha1 has a putative domain structure of three homologous cysteine-rich domains, where domains 2 and 3 make up a central domain responsible for GDNF binding. We report here the 1.8 A crystal structure of GFRalpha1 domain 3 showing a new protein fold. It is an all-alpha five-helix bundle with five disulfide bridges. The structure was used to model the homologous domain 2, the other half of the GDNF-binding fragment, and to construct the first structural model of the GDNF-GFRalpha1 interaction. Using site-directed mutagenesis, we identified closely spaced residues, Phe213, Arg224, Arg225 and Ile229, comprising a putative GDNF-binding surface. Mutating each one of them had slightly different effects on GDNF binding and RET phosphorylation. In addition, the R217E mutant bound GDNF equally well in the presence and absence of RET. Arg217 may thus be involved in the allosteric properties of GFRalpha1 or in binding RET.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15044950}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15044950 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15044950}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: All-alpha]] | | [[Category: All-alpha]] |
| [[Category: Cys-rich]] | | [[Category: Cys-rich]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:59:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:08:27 2008'' |
