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New page: left|200px<br /> <applet load="2d11" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d11, resolution 2.81Å" /> '''Crystal structure o...
 
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[[Image:2d11.gif|left|200px]]<br />
<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==
==Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide==
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.
<StructureSection load='2d11' size='340' side='right'caption='[[2d11]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2d11]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D11 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]] 2.81&#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=2d11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d11 OCA], [https://pdbe.org/2d11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d11 RCSB], [https://www.ebi.ac.uk/pdbsum/2d11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d11 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/2d11_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2d11 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Radixin|Radixin]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for NHERF recognition by ERM proteins., Terawaki S, Maesaki R, Hakoshima T, Structure. 2006 Apr;14(4):777-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16615918 16615918]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Hakoshima T]]
[[Category: Hakoshima, T.]]
[[Category: Maesaki R]]
[[Category: Maesaki, R.]]
[[Category: Terawaki S]]
[[Category: Terawaki, S.]]
[[Category: protein-peptide complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:15 2007''

Latest revision as of 13:45, 13 March 2024

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

2d11, resolution 2.81Å

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