2d11: Difference between revisions

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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 16:45, 13 March 2024

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

Structural highlights

2d11 is a 8 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.81Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RADI_MOUSE Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2d11, resolution 2.81Å

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