2f31

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2f31" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f31, resolution 2.10&Aring;" /> '''Crystal structure of...)
Current revision (09:21, 14 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2f31.gif|left|200px]]<br /><applet load="2f31" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2f31, resolution 2.10&Aring;" />
 
-
'''Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex'''<br />
 
-
==Overview==
+
==Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex==
-
Diaphanous-related formins (DRFs) regulate the nucleation and, polymerization of unbranched actin filaments. The activity of DRFs is, inhibited by an intramolecular interaction between their N-terminal, regulatory region and a conserved C-terminal segment termed the Diaphanous, autoinhibitory domain (DAD). Binding of GTP bound Rho to the mDia1 N, terminus releases this autoinhibitory restraint. Here, we describe the, crystal structure of the DAD segment of mDia1 in complex with the relevant, N-terminal fragment, termed the DID domain. The structure reveals that the, DAD segment forms an amphipathic helix that binds a conserved, concave, surface on the DID domain. Comparison with the structure of the mDia1 N, terminus bound to RhoC suggests that release of the autoinhibitory DAD, interaction is accomplished largely by Rho-induced restructuring of the, adjacent GTPase binding subdomain (GBD), but also by electrostatic, repulsion and a small, direct steric occlusion of the DAD binding cleft by, Rho itself.
+
<StructureSection load='2f31' size='340' side='right'caption='[[2f31]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[2f31]] 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=2F31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F31 FirstGlance]. <br>
-
2F31 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=2F31 OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=2f31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f31 OCA], [https://pdbe.org/2f31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f31 RCSB], [https://www.ebi.ac.uk/pdbsum/2f31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f31 ProSAT]</span></td></tr>
-
==Reference==
+
</table>
-
Structure of the autoinhibitory switch in formin mDia1., Nezami AG, Poy F, Eck MJ, Structure. 2006 Feb;14(2):257-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16472745 16472745]
+
== Function ==
 +
[https://www.uniprot.org/uniprot/Q3US76_MOUSE Q3US76_MOUSE]
 +
== 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/f3/2f31_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=2f31 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Protein complex]]
+
[[Category: Eck MJ]]
-
[[Category: Eck, M.J.]]
+
[[Category: Nezami AG]]
-
[[Category: Nezami, A.G.]]
+
[[Category: Poy F]]
-
[[Category: Poy, F.]]
+
-
[[Category: armadillo repeats]]
+
-
[[Category: formin]]
+
-
[[Category: mdia1]]
+
-
[[Category: protein-protein complex]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:19:50 2007''
+

Current revision

Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex

PDB ID 2f31

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/2f31"
Personal tools