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[[Image:1nu2.jpg|left|200px]]


{{Structure
==Crystal structure of the murine Disabled-1 (Dab1) PTB domain-ApoER2 peptide-PI-4,5P2 ternary complex==
|PDB= 1nu2 |SIZE=350|CAPTION= <scene name='initialview01'>1nu2</scene>, resolution 1.90&Aring;
<StructureSection load='1nu2' size='340' side='right'caption='[[1nu2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
<table><tr><td colspan='2'>[[1nu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NU2 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE= DAB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu2 OCA], [https://pdbe.org/1nu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1nu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nu2 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1ntv|1NTV]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu2 OCA], [http://www.ebi.ac.uk/pdbsum/1nu2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nu2 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/DAB1_MOUSE DAB1_MOUSE] Adapter molecule functioning in neural development. May regulate SIAH1 activity.<ref>PMID:9009273</ref>
 
== Evolutionary Conservation ==
'''Crystal structure of the murine Disabled-1 (Dab1) PTB domain-ApoER2 peptide-PI-4,5P2 ternary complex'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nu/1nu2_consurf.spt"</scriptWhenChecked>
Formation of the mammalian six-layered neocortex depends on a signaling pathway that involves Reelin, the very low-density lipoprotein receptor, the apolipoprotein E receptor-2 (ApoER2), and the adaptor protein Disabled-1 (Dab1). The 1.5 A crystal structure of a complex between the Dab1 phosphotyrosine binding (PTB) domain and a 14-residue peptide from the ApoER2 tail explains the unusual preference of Dab1 for unphosphorylated tyrosine within the NPxY motif of the peptide. Crystals of the complex soaked with the phosphoinositide PI-4,5P(2) (PI) show that PI binds to conserved basic residues on the PTB domain opposite the peptide binding groove. This finding explains how the Dab1 PTB domain can simultaneously bind PI and the ApoER2 tail. Recruitment of the Dab1 PTB domain to PI-rich regions of the plasma membrane may facilitate association with the Reelin receptor cytoplasmic tails to transduce a critical positional cue to migrating neurons.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1NU2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU2 OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nu2 ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes., Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC, Structure. 2003 May;11(5):569-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12737822 12737822]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Blacklow SC]]
[[Category: Blacklow, S C.]]
[[Category: Eck MJ]]
[[Category: Eck, M J.]]
[[Category: Herz J]]
[[Category: Herz, J.]]
[[Category: Jeon H]]
[[Category: Jeon, H.]]
[[Category: Song HK]]
[[Category: Song, H K.]]
[[Category: Stolt PC]]
[[Category: Stolt, P C.]]
[[Category: beta-sandwich]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:35:31 2008''

Latest revision as of 16:28, 13 March 2024

Crystal structure of the murine Disabled-1 (Dab1) PTB domain-ApoER2 peptide-PI-4,5P2 ternary complexCrystal structure of the murine Disabled-1 (Dab1) PTB domain-ApoER2 peptide-PI-4,5P2 ternary complex

Structural highlights

1nu2 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAB1_MOUSE Adapter molecule functioning in neural development. May regulate SIAH1 activity.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Howell BW, Gertler FB, Cooper JA. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO J. 1997 Jan 2;16(1):121-32. PMID:9009273 doi:http://dx.doi.org/10.1093/emboj/16.1.121

1nu2, resolution 1.90Å

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