3CVE

Crystal Structure of the carboxy terminus of Homer1

Summary for 3CVE

• Entry DOI: 10.2210/pdb3cve/pdb
• Related: 3CVF
• Descriptor: Homer protein homolog 1 (2 entities in total)
• Functional Keywords: coiled coil, alternative splicing, cell junction, cytoplasm, membrane, postsynaptic cell membrane, synapse, signaling protein
• Biological source: Rattus norvegicus (Rat)
• Cellular location: Cytoplasm : Q9Z214
• Total number of polymer chains: 4
• Total formula weight: 33856.84

Authors

Hayashi, M.K.,Stearns, M.H.,Giannini, V.,Xu, R.-M.,Sala, C.,Hayashi, Y. (deposition date: 2008-04-18, release date: 2009-03-31, Last modification date: 2024-10-16)

Primary citation

Hayashi, M.K.,Tang, C.,Verpelli, C.,Narayanan, R.,Stearns, M.H.,Xu, R.M.,Li, H.,Sala, C.,Hayashi, Y.
The postsynaptic density proteins Homer and Shank form a polymeric network structure.
Cell(Cambridge,Mass.), 137:159-171, 2009

PubMed Abstract: The postsynaptic density (PSD) is crucial for synaptic functions, but the molecular architecture retaining its structure and components remains elusive. Homer and Shank are among the most abundant scaffolding proteins in the PSD, working synergistically for maturation of dendritic spines. Here, we demonstrate that Homer and Shank, together, form a mesh-like matrix structure. Crystallographic analysis of this region revealed a pair of parallel dimeric coiled coils intercalated in a tail-to-tail fashion to form a tetramer, giving rise to the unique configuration of a pair of N-terminal EVH1 domains at each end of the coiled coil. In neurons, the tetramerization is required for structural integrity of the dendritic spines and recruitment of proteins to synapses. We propose that the Homer-Shank complex serves as a structural framework and as an assembly platform for other PSD proteins.

PubMed: 19345194
DOI: 10.1016/j.cell.2009.01.050

Experimental method

X-RAY DIFFRACTION (1.75 Å)