1DDW

HOMER EVH1 DOMAIN UNLIGANDED

Summary for 1DDW

• Entry DOI: 10.2210/pdb1ddw/pdb
• Related: 1DDV
• Descriptor: GLGF-DOMAIN PROTEIN HOMER (2 entities in total)
• Functional Keywords: pleckstrin homology domain fold, signaling protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm : Q9Z214
• Total number of polymer chains: 1
• Total formula weight: 13827.22

Authors

Beneken, J.,Tu, J.C.,Xiao, B.,Worley, P.F.,Leahy, D.J. (deposition date: 1999-11-11, release date: 2000-05-10, Last modification date: 2017-10-04)

Primary citation

Beneken, J.,Tu, J.C.,Xiao, B.,Nuriya, M.,Yuan, J.P.,Worley, P.F.,Leahy, D.J.
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition.
Neuron, 26:143-154, 2000

PubMed Abstract: Homer EVH1 (Ena/VASP Homology 1) domains interact with proline-rich motifs in the cytoplasmic regions of group 1 metabotropic glutamate receptors (mGluRs), inositol-1,4,5-trisphosphate receptors (IP3Rs), and Shank proteins. We have determined the crystal structure of the Homer EVH1 domain complexed with a peptide from mGluR (TPPSPF). In contrast to other EVH1 domains, the bound mGluR ligand assumes an unusual conformation in which the side chains of the Ser-Pro tandem are oriented away from the Homer surface, and the Phe forms a unique contact. This unusual binding mode rationalizes conserved features of both Homer and Homer ligands that are not shared by other EVH1 domains. Site-directed mutagenesis confirms the importance of specific Homer residues for ligand binding. These results establish a molecular basis for understanding the biological properties of Homer-ligand complexes.

PubMed: 10798399
DOI: 10.1016/S0896-6273(00)81145-9

Experimental method

X-RAY DIFFRACTION (1.7 Å)