2d1k

From Proteopedia

(Difference between revisions)

Revision as of 06:32, 30 May 2018

Ternary complex of the WH2 domain of mim with actin-dnase I

Structural highlights

2d1k is a 3 chain structure with sequence from Bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Related:	2a3z, 2a40, 2a41, 2a42, 2d1l
Activity:	Deoxyribonuclease I, with EC number 3.1.21.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [MTSS1_HUMAN] May be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. [DNAS1_BOVIN] Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity).

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 adaptor protein missing-in-metastasis (MIM) contains independent F- and G-actin binding domains, consisting, respectively, of an N-terminal 250 aa IRSp53/MIM homology domain (IMD) and a C-terminal WASP-homology domain 2 (WH2). We determined the crystal structures of MIM's IMD and that of its WH2 bound to actin. The IMD forms a dimer, with each subunit folded as an antiparallel three-helix bundle. This fold is related to that of the BAR domain. Like the BAR domain, the IMD has been implicated in membrane binding. Yet, comparison of the structures reveals that the membrane binding surfaces of the two domains have opposite curvatures, which may determine the type of curvature of the interacting membrane. The WH2 of MIM is longer than the prototypical WH2, interacting with all four subdomains of actin. We characterize a similar WH2 at the C terminus of IRSp53 and propose that in these two proteins WH2 performs a scaffolding function.

Structural basis for the actin-binding function of missing-in-metastasis.,Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R Structure. 2007 Feb;15(2):145-55. PMID:17292833^[1]

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

References

↑ Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R. Structural basis for the actin-binding function of missing-in-metastasis. Structure. 2007 Feb;15(2):145-55. PMID:17292833 doi:10.1016/j.str.2006.12.005

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/2d1k"

@@ Line 1: / Line 1: @@
 ==Ternary complex of the WH2 domain of mim with actin-dnase I==
 <StructureSection load='2d1k' size='340' side='right' caption='[[2d1k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a3z|2a3z]], [[2a40|2a40]], [[2a41|2a41]], [[2a42|2a42]], [[2d1l|2d1l]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </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=2d1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1k OCA], [http://pdbe.org/2d1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d1k RCSB], [http://www.ebi.ac.uk/pdbsum/2d1k 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=2d1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1k OCA], [http://pdbe.org/2d1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d1k RCSB], [http://www.ebi.ac.uk/pdbsum/2d1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1k ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/2d1k_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/2d1k_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2d1k

From Proteopedia

Revision as of 06:32, 30 May 2018

Ternary complex of the WH2 domain of mim with actin-dnase I

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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