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| | <StructureSection load='1nu2' size='340' side='right'caption='[[1nu2]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1nu2' size='340' side='right'caption='[[1nu2]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1NU2 FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ntv|1ntv]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu2 OCA], [http://pdbe.org/1nu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1nu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nu2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DAB1_MOUSE DAB1_MOUSE]] Adapter molecule functioning in neural development. May regulate SIAH1 activity.<ref>PMID:9009273</ref> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Blacklow, S C]] | + | [[Category: Blacklow SC]] |
| - | [[Category: Eck, M J]] | + | [[Category: Eck MJ]] |
| - | [[Category: Herz, J]] | + | [[Category: Herz J]] |
| - | [[Category: Jeon, H]] | + | [[Category: Jeon H]] |
| - | [[Category: Song, H K]] | + | [[Category: Song HK]] |
| - | [[Category: Stolt, P C]] | + | [[Category: Stolt PC]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
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.
Publication Abstract from PubMed
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.
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:12737822[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC. Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes. Structure. 2003 May;11(5):569-79. PMID:12737822
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