2d11: Difference between revisions

Revision as of 17:54, 21 February 2008

Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide

OverviewOverview

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.

About this StructureAbout this Structure

2D11 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:54:17 2008

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OCA

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 '''Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-D11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D11 OCA].
+D11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D11 OCA].
 ==Reference==
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 [[Category: protein-peptide complex]]
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