1ddw: Difference between revisions
New page: left|200px<br /><applet load="1ddw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddw, resolution 1.70Å" /> '''HOMER EVH1 DOMAIN UN... |
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[[Image:1ddw.gif|left|200px]]<br /><applet load="1ddw" size=" | [[Image:1ddw.gif|left|200px]]<br /><applet load="1ddw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ddw, resolution 1.70Å" /> | caption="1ddw, resolution 1.70Å" /> | ||
'''HOMER EVH1 DOMAIN UNLIGANDED'''<br /> | '''HOMER EVH1 DOMAIN UNLIGANDED'''<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== | ||
1DDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | 1DDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1DDW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[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: pleckstrin homology domain fold]] | [[Category: pleckstrin homology domain fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:37 2008'' | ||
Revision as of 10:15, 21 February 2008
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HOMER EVH1 DOMAIN UNLIGANDED
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
1DDW is a Single protein structure of sequence 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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