This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2d2q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2d2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d2q, resolution 2.8&Aring;" /> '''Crystal structure of ...)
Current revision (13:45, 13 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2d2q.gif|left|200px]]<br /><applet load="2d2q" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2d2q, resolution 2.8&Aring;" />
 
-
'''Crystal structure of the dimerized radixin FERM domain'''<br />
 
-
==Overview==
+
==Crystal structure of the dimerized radixin FERM domain==
-
ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of, adhesion molecules in the formation of the membrane-associated, cytoskeleton. The binding site is located in the FERM (4.1 and ERM), domain, a domain that is masked in the inactive form. A conventional, masking motif, strand 1 (residues 494-500 in radixin), has previously been, identified in the C-terminal tail domain. Here, the crystal structure of, dimerized radixin FERM domains (residues 1-310) is presented in which the, binding site of one molecule is occupied by the C-terminal residues, (residues 295-304, strand 2) of the other molecule. The residues contain a, conserved motif that is compatible with that identified in the adhesion, molecules. The residues might serve as a second masking region in the, inactive form of ERM proteins.
+
<StructureSection load='2d2q' size='340' side='right'caption='[[2d2q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2d2q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2Q 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]] 2.8&#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=2d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2q OCA], [https://pdbe.org/2d2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d2q RCSB], [https://www.ebi.ac.uk/pdbsum/2d2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d2q 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/d2/2d2q_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=2d2q ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
2D2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2D2Q OCA].
+
*[[Radixin|Radixin]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304., Kitano K, Yusa F, Hakoshima T, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16582480 16582480]
+
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Hakoshima T]]
-
[[Category: Hakoshima, T.]]
+
[[Category: Kitano K]]
-
[[Category: Kitano, K.]]
+
[[Category: Yusa F]]
-
[[Category: Yusa, F.]]
+
-
[[Category: homo dimer]]
+
-
[[Category: masking]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:24:25 2007''
+

Current revision

Crystal structure of the dimerized radixin FERM domain

PDB ID 2d2q

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d2q"
Personal tools