2d11

From Proteopedia

(Difference between revisions)

Revision as of 06:36, 30 May 2018

Crystal 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 Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1gc7, 1gc6, 1j19, 1isn, 2d10
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. [NHRF2_HUMAN] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.^[1] ^[2]

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^[3]

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

References

↑ Yun CH, Oh S, Zizak M, Steplock D, Tsao S, Tse CM, Weinman EJ, Donowitz M. cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3010-5. PMID:9096337
↑ Zizak M, Lamprecht G, Steplock D, Tariq N, Shenolikar S, Donowitz M, Yun CH, Weinman EJ. cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger 3 (NHE3) are dependent on the presence but not the phosphorylation of NHE regulatory factor. J Biol Chem. 1999 Aug 27;274(35):24753-8. PMID:10455146
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d11"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide==
 <StructureSection load='2d11' size='340' side='right' caption='[[2d11]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2d11]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D11 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc7|1gc7]], [[1gc6|1gc6]], [[1j19|1j19]], [[1isn|1isn]], [[2d10|2d10]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d11 OCA], [http://pdbe.org/2d11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d11 RCSB], [http://www.ebi.ac.uk/pdbsum/2d11 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d11 OCA], [http://pdbe.org/2d11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d11 RCSB], [http://www.ebi.ac.uk/pdbsum/2d11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d11 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/2d11_consurf.spt"</scriptWhenChecked>
+    <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>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 2d11" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Radixin|Radixin]]
 == References ==
 <references/>

2d11

From Proteopedia

Revision as of 06:36, 30 May 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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