View source for 3p40


==Crystal structure of neurofascin adhesion complex in space group p3221==
<StructureSection load='3p40' size='340' side='right'caption='[[3p40]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3p40]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P40 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[3p3y|3p3y]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFASC, KIAA0756 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3p40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p40 OCA], [https://pdbe.org/3p40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p40 RCSB], [https://www.ebi.ac.uk/pdbsum/3p40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p40 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/NFASC_HUMAN NFASC_HUMAN]] Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions (By similarity). 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The L1 family neural cell adhesion molecules play key roles in specifying the formation and remodeling of the neural network, but their homophilic interaction that mediates adhesion is not well understood. We report two crystal structures of a dimeric form of the headpiece of neurofascin, an L1 family member. The four N-terminal Ig-like domains of neurofascin form a horseshoe shape, akin to several other immunoglobulin superfamily cell adhesion molecules such as hemolin, axonin, and Dscam. The neurofascin dimer, captured in two crystal forms with independent packing patterns, reveals a pair of horseshoes in trans-synaptic adhesion mode. The adhesion interaction is mediated mostly by the second Ig-like domain, which features an intermolecular beta-sheet formed by the joining of two individual GFC beta-sheets and a large but loosely packed hydrophobic cluster. Mutagenesis combined with gel filtration assays suggested that the side chain hydrogen bonds at the intermolecular beta-sheet are essential for the homophilic interaction and that the residues at the hydrophobic cluster play supplementary roles. Our structures reveal a conserved homophilic adhesion mode for the L1 family and also shed light on how the pathological mutations of L1 affect its structure and function.

Homophilic adhesion mechanism of neurofascin, a member of the L1 family of neural cell adhesion molecules.,Liu H, Focia PJ, He X J Biol Chem. 2011 Jan 7;286(1):797-805. Epub 2010 Nov 3. PMID:21047790<ref>PMID:21047790</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3p40" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: He, X]]
[[Category: Liu, H]]
[[Category: Cell adhesion]]
[[Category: Ig domain]]