1ddw: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ddw.gif|left|200px]] | [[Image:1ddw.gif|left|200px]] | ||
'''HOMER EVH1 DOMAIN UNLIGANDED''' | {{Structure | ||
|PDB= 1ddw |SIZE=350|CAPTION= <scene name='initialview01'>1ddw</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HOMER EVH1 DOMAIN UNLIGANDED''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1DDW is a [ | 1DDW is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10798399 10798399] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: pleckstrin homology domain fold]] | [[Category: pleckstrin homology domain fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:36:56 2008'' | ||
Revision as of 08:36, 20 March 2008
| |||||||||||||
| 1ddw, resolution 1.70Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
Page seeded by OCA on Thu Mar 20 10:36:56 2008