2d11: Difference between revisions

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[[Image:2d11.gif|left|200px]]<br />

[[Image:2d11.gif|left|200px]]<br /><applet load="2d11" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2d11" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2d11, resolution 2.81Å" />

'''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==

2D11 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].

2D11 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]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12~~ 21:25:~~15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:17 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2d11.gif|left|200px]]<br />
+[[Image:2d11.gif|left|200px]]<br /><applet load="2d11" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2d11" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2d11, resolution 2.81&Aring;" />
 '''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==
@@ Line 19: / Line 18: @@
 [[Category: protein-peptide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:17 2008''