Search results for "SNX9"

showing 2 items of 2 documents

Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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HACANCOi : a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins

2020

AbstractUnidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T2) relaxation times allowing sophisticated coherence transfer pathway selection in comparison to folded proteins. 1Hα-detection ensures non-susceptibility to chemical exchange with the solvent and enables chemical shift assignment of consecutive proline residues, typically abundant in IDPs. However, many IDPs undergo a disorder-to-order transition upon interaction with their target protein, which leads to the loss of the favorable relaxation properties. Long coherence transfer routes now result in prohibitively large dec…

chemistry.chemical_classificationSpinsbiologyChemistryGlobular proteinRelaxation (NMR)E. coliIDPGB1Intrinsically disordered proteinsintrinsically disordered proteinBiochemistryResonance (particle physics)Chemical physicsSNX9 SH3biology.proteinTarget proteinProtein GproteiinitNMR-spektroskopiaSpectroscopyEspFresonance assignmentCoherence (physics)
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