2d1l: Difference between revisions

Revision as of 11:33, 22 May 2024

Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)

Structural highlights

2d1l is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	MSE
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MTSS1_MOUSE Inhibits the nucleation of actin filaments in vitro.^[1]

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^[2]

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

References

↑ Mattila PK, Salminen M, Yamashiro T, Lappalainen P. Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain. J Biol Chem. 2003 Mar 7;278(10):8452-9. Epub 2002 Dec 13. PMID:12482861 doi:https://dx.doi.org/10.1074/jbc.M212113200
↑ 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

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OCA

[1] Mattila PK, Salminen M, Yamashiro T, Lappalainen P. Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain. J Biol Chem. 2003 Mar 7;278(10):8452-9. Epub 2002 Dec 13. PMID:12482861 doi:https://dx.doi.org/10.1074/jbc.M212113200

[2] 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]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='2d1l' size='340' side='right'caption='[[2d1l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d1l]] is a 2 chain structure with sequence from [https://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=2D1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d1l]] 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=2D1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1L FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2d1k|2d1k]], [[1y2o|1y2o]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mtss1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2d1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1l OCA], [https://pdbe.org/2d1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d1l RCSB], [https://www.ebi.ac.uk/pdbsum/2d1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MTSS1_MOUSE MTSS1_MOUSE]] Inhibits the nucleation of actin filaments in vitro.<ref>PMID:12482861</ref>
+[https://www.uniprot.org/uniprot/MTSS1_MOUSE MTSS1_MOUSE] Inhibits the nucleation of actin filaments in vitro.<ref>PMID:12482861</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 34: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Chereau, D]]
+[[Category: Chereau D]]
-[[Category: Dominguez, R]]
+[[Category: Dominguez R]]
-[[Category: Ferron, F]]
+[[Category: Ferron F]]
-[[Category: Kerff, F]]
+[[Category: Kerff F]]
-[[Category: Lee, S H]]
+[[Category: Lee SH]]
-[[Category: Actin binding]]
-[[Category: Imd]]
-[[Category: Irsp53]]
-[[Category: Protein binding]]

2d1l: Difference between revisions

Revision as of 11:33, 22 May 2024

Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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