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PMID:26853939
| Citation |
Croll, TI, Smith, BJ, Margetts, MB, Whittaker, J, Weiss, MA, Ward, CW and Lawrence, MC (2016) Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain. Structure 24:469-76 |
|---|---|
| Abstract |
Insulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 Å) structure currently exists for the IR ectodomain, with some segments ill-defined or unmodeled due to disorder. Here, we revise this structure using new diffraction data to 3.3 Å resolution that allow improved modeling of the N-linked glycans, the first and third fibronectin type III domains, and the insert domain. A novel haptic interactive molecular dynamics strategy was used to aid fitting to low-resolution electron density maps. The resulting model provides a foundation for investigation of structural transitions in IR upon ligand binding. |
| Links |
PubMed PMC4860004 Online version:10.1016/j.str.2015.12.014 |
| Keywords |
Antigens, CD/chemistry; Antigens, CD/metabolism; Binding Sites; Crystallography, X-Ray; Fibronectins/metabolism; Humans; Models, Molecular; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Receptor, Insulin/chemistry; Receptor, Insulin/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0042802: identical protein binding |
ECO:0000353: physical interaction evidence used in manual assertion |
UniProtKB:P06213-1 |
F |
Seeded From UniProt |
complete | ||
Notes
See also
References
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