9QUX
Solution structure of the Homer1 EVH1 domain
Summary for 9QUX
| Entry DOI | 10.2210/pdb9qux/pdb |
| NMR Information | BMRB: 34990 |
| Descriptor | Homer protein homolog 1 (1 entity in total) |
| Functional Keywords | postsynapse, enabled/vasp homology 1 domain, peptide binding protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 13757.41 |
| Authors | Czajlik, A.,Maruzs, B.,Fanni, F.,Batta, G.,Gaspari, Z.,Peterfia, B.F. (deposition date: 2025-04-11, release date: 2025-12-03) |
| Primary citation | Kalman, Z.E.,Czajlik, A.,Maruzs, B.,Farkas, F.,Pap, I.,Homonnay, C.,Klumpler, T.,Batta, G.,Gaspari, Z.,Peterfia, B. Structural Modeling and Dynamics of the Full-Length Homer1 Multimer. Proteins, 2025 Cited by PubMed Abstract: Homer proteins are modular scaffold molecules that constitute an integral part of the protein network within the postsynaptic density. Full-length Homer1 forms a large homotetramer via a long coiled coil region, and can interact with proline-rich target sequences with its globular EVH1 domain. Here we report an atomistic model of the Homer1 coiled coil region along with the NMR solution structure and backbone dynamics of its EVH1 domain, with implications for the organization of the full-length tetramer. Compared to the already available EVH1 structures, our NMR ensemble exhibits subtle differences, mostly in and around its partner binding region, suggesting the presence of ligand-induced conformational transitions. Molecular dynamics simulations of the long coiled coil reveal distinct regions with different stability and flexibility, with the N-terminal part of the coiled coil exhibiting the largest motions. Interestingly, this segment is highly conserved, pointing to the functional relevance of the observed dynamical features. Our results indicate previously unexplored aspects of the flexibility of the full-length Homer1 tetramer that might contribute to the dynamic rearrangements of the postsynaptic protein network linked to its functional transitions. PubMed: 41267651DOI: 10.1002/prot.70091 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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