View source for 6f2o


==Crystal structure of mouse SALM5 adhesion protein extracellular LRR-Ig domain fragment==
<StructureSection load='6f2o' size='340' side='right'caption='[[6f2o]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6f2o]] is a 1 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=6F2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F2O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=6f2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2o OCA], [https://pdbe.org/6f2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f2o RCSB], [https://www.ebi.ac.uk/pdbsum/6f2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LRFN5_MOUSE LRFN5_MOUSE] Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Synaptic adhesion molecules play a crucial role in the regulation of synapse development and maintenance. Recently, several families of leucine-rich repeat (LRR) domain-containing neuronal adhesion molecules have been characterised, including netrin-G ligands, LRRTMs and the synaptic adhesion-like molecule (SALM) family proteins. Most of these are expressed at the excitatory glutamatergic synapses, and dysfunctions of these genes are genetically linked with cognitive disorders, such as autism spectrum disorders and schizophrenia. The SALM family proteins SALM3 and SALM5, similar to SLITRKs, have been shown to bind to the presynaptic receptor protein tyrosine phosphatase (RPTP) family ligands. Here, we present the 3.1 A crystal structure of the SALM5 LRR-Ig-domain construct and biophysical studies that verify the crystallographic results. We show that SALM1, SALM3 and SALM5 form similar dimeric structures, in which the LRR domains form the dimer interface. Both SALM3 and SALM5 bind to RPTP immunoglobulin domains with micromolar affinity. SALM3 shows a clear preference for the RPTP ligands with the meB splice insert. Our structural studies and sequence conservation analysis suggests a ligand-binding site and mechanism for RPTP binding via the dimeric LRR domain region.

The structure of SALM5 suggests a dimeric assembly for the presynaptic RPTP ligand recognition.,Karki S, Paudel P, Sele C, Shkumatov AV, Kajander T Protein Eng Des Sel. 2018 Jun 12. pii: 5036097. doi: 10.1093/protein/gzy012. PMID:29897575<ref>PMID:29897575</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6f2o" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Kajander T]]
[[Category: Karki S]]
[[Category: Paudel P]]
[[Category: Sele C]]