2d10: Difference between revisions

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{{Seed}}
[[Image:2d10.png|left|200px]]


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==Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide==
The line below this paragraph, containing "STRUCTURE_2d10", creates the "Structure Box" on the page.
<StructureSection load='2d10' size='340' side='right'caption='[[2d10]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2d10]] 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=2D10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D10 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d10 OCA], [https://pdbe.org/2d10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d10 RCSB], [https://www.ebi.ac.uk/pdbsum/2d10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d10 ProSAT]</span></td></tr>
{{STRUCTURE_2d10|  PDB=2d10  |  SCENE=  }}
</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/d1/2d10_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=2d10 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide===
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>
</div>
<div class="pdbe-citations 2d10" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16615918}}, adds the Publication Abstract to the page
*[[Radixin|Radixin]]
(as it appears on PubMed at http://www.pubmed.gov), where 16615918 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16615918}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Homo sapiens]]
2D10 is a [[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=2D10 OCA].
[[Category: Large Structures]]
 
==Reference==
Structural basis for NHERF recognition by ERM proteins., Terawaki S, Maesaki R, Hakoshima T, Structure. 2006 Apr;14(4):777-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16615918 16615918]
 
Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF)., Terawaki S, Maesaki R, Okada K, Hakoshima T, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):177-9. Epub 2002, Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12499563 12499563]
 
Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain., Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T, EMBO J. 2000 Sep 1;19(17):4449-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10970839 10970839]
 
Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex., Hamada K, Shimizu T, Yonemura S, Tsukita S, Tsukita S, Hakoshima T, EMBO J. 2003 Feb 3;22(3):502-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554651 12554651]
[[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://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:58:48 2008''

Latest revision as of 11:22, 25 October 2023

Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptideCrystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide

Structural highlights

2d10 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 2.5Å
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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Terawaki S, Maesaki R, Hakoshima T. Structural basis for NHERF recognition by ERM proteins. Structure. 2006 Apr;14(4):777-89. PMID:16615918 doi:10.1016/j.str.2006.01.015

2d10, resolution 2.50Å

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