7OJ9
NMR solution structure of SNX9 SH3 - EEEV nsP3 peptide complex
Summary for 7OJ9
| Entry DOI | 10.2210/pdb7oj9/pdb |
| NMR Information | BMRB: 34628 |
| Descriptor | EEEV nsP3 peptide, Sorting nexin-9 (2 entities in total) |
| Functional Keywords | complex, endocytosis |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 9727.98 |
| Authors | Tossavainen, H.,Permi, P. (deposition date: 2021-05-14, release date: 2022-04-13, Last modification date: 2024-06-19) |
| Primary citation | Tossavainen, H.,Ugurlu, H.,Karjalainen, M.,Hellman, M.,Antenucci, L.,Fagerlund, R.,Saksela, K.,Permi, P. 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. Structure, 30:828-, 2022 Cited by PubMed Abstract: Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]xØPxxP, the hydrophobic residue Ø being proline or leucine. We have studied the unusual Ø = 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 RxAPxxP motif was also found in human T cell leukemia virus-1 (HTLV-1) Gag polyprotein. We found that this motif was required for efficient HTLV-1 infection, and that the specificity of SNX9 SH3 for the RxAPxxP core binding motif was importantly involved in this process. PubMed: 35390274DOI: 10.1016/j.str.2022.03.006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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