1ddv
From Proteopedia
(New page: 200px<br /><applet load="1ddv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddv, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ddv.gif|left|200px]]<br /><applet load="1ddv" size=" | + | [[Image:1ddv.gif|left|200px]]<br /><applet load="1ddv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ddv, resolution 1.90Å" /> | caption="1ddv, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HOMER EVH1 DOMAIN WITH BOUND MGLUR PEPTIDE'''<br /> | '''CRYSTAL STRUCTURE OF THE HOMER EVH1 DOMAIN WITH BOUND MGLUR PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Homer EVH1 (Ena/VASP Homology 1) domains interact with proline-rich motifs | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DDV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1DDV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Beneken, J.]] | [[Category: Beneken, J.]] | ||
| - | [[Category: Leahy, D | + | [[Category: Leahy, D J.]] |
| - | [[Category: Tu, J | + | [[Category: Tu, J C.]] |
| - | [[Category: Worley, P | + | [[Category: Worley, P F.]] |
[[Category: Xiao, B.]] | [[Category: Xiao, B.]] | ||
[[Category: beta turn]] | [[Category: beta turn]] | ||
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[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:36 2008'' |
Revision as of 10:15, 21 February 2008
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CRYSTAL STRUCTURE OF THE HOMER EVH1 DOMAIN WITH BOUND MGLUR PEPTIDE
Overview
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.
About this Structure
1DDV is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition., Beneken J, Tu JC, Xiao B, Nuriya M, Yuan JP, Worley PF, Leahy DJ, Neuron. 2000 Apr;26(1):143-54. PMID:10798399
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