2d11

<table><tr><td colspan='2'>[[2d11]] is a 8 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=2D11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D11 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc7|1gc7]], [[1gc6|1gc6]], [[1j19|1j19]], [[1isn|1isn]], [[2d10|2d10]]</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=2d11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d11 OCA], [http://pdbe.org/2d11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d11 RCSB], [http://www.ebi.ac.uk/pdbsum/2d11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d11 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE]] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [[http://www.uniprot.org/uniprot/NHRF2_HUMAN NHRF2_HUMAN]] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.<ref>PMID:9096337</ref> <ref>PMID:10455146</ref>

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== Publication Abstract from PubMed ==

The Na+/H+ exchanger regulatory factor (NHERF) is a key adaptor protein involved in the anchoring of ion channels and receptors to the actin cytoskeleton through binding to ERM (ezrin/radixin/moesin) proteins. NHERF binds the FERM domain of ERM proteins, although NHERF has no signature Motif-1 sequence for FERM binding found in adhesion molecules. The crystal structures of the radixin FERM domain complexed with the NHERF-1 and NHERF-2 C-terminal peptides revealed a peptide binding site of the FERM domain specific for the 13 residue motif MDWxxxxx(L/I)Fxx(L/F) (Motif-2), which is distinct from Motif-1. This Motif-2 forms an amphipathic alpha helix for hydrophobic docking to subdomain C of the FERM domain. This docking causes induced-fit conformational changes in subdomain C and affects binding to adhesion molecule peptides, while the two binding sites are not overlapped. Our studies provide structural paradigms for versatile ERM linkages between membrane proteins and the cytoskeleton.

Structural basis for NHERF recognition by ERM proteins.,Terawaki S, Maesaki R, Hakoshima T Structure. 2006 Apr;14(4):777-89. PMID:16615918<ref>PMID:16615918</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Hakoshima, T]]

[[Category: Maesaki, R]]

[[Category: Terawaki, S]]

[[Category: Protein-peptide complex]]