2xb6
From Proteopedia
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| - | + | ==REVISITED CRYSTAL STRUCTURE OF NEUREXIN1BETA-NEUROLIGIN4 COMPLEX== | |
| - | === | + | <StructureSection load='2xb6' size='340' side='right' caption='[[2xb6]], [[Resolution|resolution]] 2.60Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2xb6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XB6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c4r|1c4r]], [[2vh8|2vh8]], [[2wqz|2wqz]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xb6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xb6 RCSB], [http://www.ebi.ac.uk/pdbsum/2xb6 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/NLGNX_HUMAN NLGNX_HUMAN]] Defects in NLGN4X may be the cause of susceptibility to autism X-linked type 2 (AUTSX2) [MIM:[http://omim.org/entry/300495 300495]]. AUTSX2 is a pervasive developmental disorder (PDD), prototypically characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age.<ref>PMID:12669065</ref> Defects in NLGN4X may be the cause of susceptibility to X-linked Asperger syndrome 2 (ASPGX2) [MIM:[http://omim.org/entry/300497 300497]]. ASPGX2 is considered to be a form of childhood autism. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NLGNX_HUMAN NLGNX_HUMAN]] Putative neuronal cell surface protein involved in cell-cell-interactions. [[http://www.uniprot.org/uniprot/NRX1B_RAT NRX1B_RAT]] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).<ref>PMID:9325340</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xb/2xb6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The extracellular domains of neuroligins and neurexins interact through Ca(2+) to form flexible trans-synaptic associations characterized by selectivity for neuroligin or neurexin subtypes. This heterophilic interaction, essential for synaptic maturation and differentiation, is regulated by gene selection, alternative mRNA splicing and post-translational modifications. A new, 2.6 A-resolution crystal structure of a soluble neurexin-1beta-neuroligin-4 (Nrx1beta-NL4) complex permits a detailed description of the Ca(2+)-coordinated interface and unveils concerted positional rearrangements of several residues of NL4, not observed in neuroligin-1, associated with Nrx1beta binding. Surface plasmon resonance analysis of the binding of structure-guided Nrx1beta mutants towards NL4 and neuroligin-1 shows that flexibility of the Nrx1beta-binding site in NL4 is reflected in a greater dissociation constant of the complex and higher sensitivity to ionic strength and pH variations. Analysis of neuroligin mutants points to critical functions for two respective residues in neuroligin-1 and neuroligin-2 in governing the affinity of the complexes. Although neuroligin-1 and neuroligin-2 have pre-determined conformations that respectively promote and prevent Nrx1beta association, unique conformational reshaping of the NL4 surface is required to permit Nrx1beta association. | ||
| - | + | Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions.,Leone P, Comoletti D, Ferracci G, Conrod S, Garcia SU, Taylor P, Bourne Y, Marchot P EMBO J. 2010 Jul 21;29(14):2461-71. Epub 2010 Jun 11. PMID:20543817<ref>PMID:20543817</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Neurexin|Neurexin]] | *[[Neurexin|Neurexin]] | ||
*[[Neuroligin|Neuroligin]] | *[[Neuroligin|Neuroligin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Bourne, Y | + | [[Category: Bourne, Y]] |
| - | [[Category: Comoletti, D | + | [[Category: Comoletti, D]] |
| - | [[Category: Conrod, S | + | [[Category: Conrod, S]] |
| - | [[Category: Ferracci, G | + | [[Category: Ferracci, G]] |
| - | [[Category: Garcia, S U | + | [[Category: Garcia, S U]] |
| - | [[Category: Leone, P | + | [[Category: Leone, P]] |
| - | [[Category: Marchot, P | + | [[Category: Marchot, P]] |
| - | [[Category: Taylor, P | + | [[Category: Taylor, P]] |
[[Category: Alpha-beta-hydrolase fold]] | [[Category: Alpha-beta-hydrolase fold]] | ||
[[Category: Autism]] | [[Category: Autism]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Conformational rearrangement]] | [[Category: Conformational rearrangement]] | ||
Revision as of 12:22, 18 December 2014
REVISITED CRYSTAL STRUCTURE OF NEUREXIN1BETA-NEUROLIGIN4 COMPLEX
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