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==Crystal structure of the FERM domain of FRMPD4==
<StructureSection load='7byj' size='340' side='right'caption='[[7byj]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BYJ 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]] 2.49&#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=7byj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byj OCA], [https://pdbe.org/7byj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7byj RCSB], [https://www.ebi.ac.uk/pdbsum/7byj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7byj ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Scaffold proteins play crucial roles in orchestrating synaptic signaling and plasticity in the excitatory synapses by providing a structural link between glutamatergic receptors, signaling molecules, and neuronal cytoskeletons. FRMPD4 is a neural scaffold protein that binds to metabotropic glutamate receptors via its FERM domain. Here, we determine the crystal structure of the FERM domain of FRMPD4 at 2.49 A resolution. The structure reveals that the canonical target binding groove of FRMPD4 FERM is occupied by a conserved fragment C-terminal to the FERM domain, suggesting that the FRMPD4-mGluR interaction may adopt a distinct binding mode. In addition, FRMPD4 FERM does not contain a typical phosphoinositide binding site at the F1/F3 cleft found in ERM family FERM domains, but it possesses a conserved basic residue cluster on the F2 lobe which could bind to lipid effectively. Finally, analysis of mutations that are associated with X-linked intellectual disability suggests that they may compromise the biological function of FRMPD4 by destabilizing the FERM structure.

Structure of the FERM domain of a neural scaffold protein FRMPD4 implicated in X-linked intellectual disability.,Wang M, Lin L, Shi Y, He L, Wang C, Zhu J Biochem J. 2020 Dec 11;477(23):4623-4634. doi: 10.1042/BCJ20200857. PMID:33216857<ref>PMID:33216857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Lin L]]
[[Category: Wang C]]
[[Category: Wang M]]
[[Category: Zhu J]]