RGD Reference Report - Structural characterization of the self-association of the death domain of p75(NTR.). - Rat Genome Database

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Structural characterization of the self-association of the death domain of p75(NTR.).

Authors: Qu, Q  Chen, J  Wang, Y  Gui, W  Wang, L  Fan, Z  Jiang, T 
Citation: Qu Q, etal., PLoS One. 2013;8(3):e57839. doi: 10.1371/journal.pone.0057839. Epub 2013 Mar 5.
RGD ID: 10413904
Pubmed: PMID:23472109   (View Abstract at PubMed)
PMCID: PMC3589453   (View Article at PubMed Central)
DOI: DOI:10.1371/journal.pone.0057839   (Journal Full-text)

The neurotrophin receptor p75(NTR) conveys multiple signals via its intracellular death domain. However, how the death domain is activated and interacts with downstream adaptors remains unclear. Here, we report two crystal structures of the p75(NTR) death domain in the form of a non-covalent asymmetric dimer and a Cys379-Cys379 disulfide bond linked symmetric dimer, respectively. These two dimer arrangements have not previously been observed in other death domain-containing proteins. Further analysis shows that both the Cys379-Cys379 disulfide linked and non-covalent full-length p75(NTR) dimers are present on the cell surface. These observations suggest that various oligomers may exist simultaneously on the cell surface, and that p75(NTR) activation and signalling may be modulated by neurotrophins or other factors via inducing a shift of the equilibrium between different oligomeric states.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding  IPINgfr (Rattus norvegicus)10413904homodimerizationRGD 

Objects Annotated

Genes (Rattus norvegicus)
Ngfr  (nerve growth factor receptor)


Additional Information