The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
Structural Basis of Rab Effector Specificity
Open accessAbstract
The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A was solved to 2.6 A resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions, which are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A. Sequence and structure analysis, and biochemical data suggest that this pocket, or Rab complementarity-determining region (RabCDR), establishes a specific interaction between each Rab protein and its effectors. RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion.
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Metadata
- Authors
- Ostermeier, C., & Brunger, A. T.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-02
- Volume
- 96
- Issue
- 3
- Pages
- 363-374
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2083067971
- Cited by
- 340
- References
- 81
- FWCI
- 12.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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