1m4j: Difference between revisions

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[[Image:1m4j.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF THE N-TERMINAL ADF-H DOMAIN OF MOUSE TWINFILIN ISOFORM-1==
The line below this paragraph, containing "STRUCTURE_1m4j", creates the "Structure Box" on the page.
<StructureSection load='1m4j' size='340' side='right'caption='[[1m4j]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1m4j]] 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=1M4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4J FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4j OCA], [https://pdbe.org/1m4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4j RCSB], [https://www.ebi.ac.uk/pdbsum/1m4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4j ProSAT]</span></td></tr>
{{STRUCTURE_1m4j| PDB=1m4j |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/TWF1_MOUSE TWF1_MOUSE] Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.<ref>PMID:9249064</ref> <ref>PMID:10669753</ref> <ref>PMID:15282541</ref> <ref>PMID:16511569</ref>
== 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/m4/1m4j_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=1m4j ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE N-TERMINAL ADF-H DOMAIN OF MOUSE TWINFILIN ISOFORM-1'''
==See Also==
 
*[[Twinfilin|Twinfilin]]
 
== References ==
==Overview==
<references/>
Twinfilin is an evolutionarily conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. It is composed of two actin-depolymerization factor homology (ADF-H) domains that show approximately 20% sequence identity to ADF/cofilin proteins. In contrast to ADF/cofilins, which bind both G-actin and F-actin and promote filament depolymerization, twinfilin interacts only with G-actin. To elucidate the molecular mechanisms of twinfilin-actin monomer interaction, we determined the crystal structure of the N-terminal ADF-H domain of twinfilin and mapped its actin-binding site by site-directed mutagenesis. This domain has similar overall structure to ADF/cofilins, and the regions important for actin monomer binding in ADF/cofilins are especially well conserved in twinfilin. Mutagenesis studies show that the N-terminal ADF-H domain of twinfilin and ADF/cofilins also interact with actin monomers through similar interfaces, although the binding surface is slightly extended in twinfilin. In contrast, the regions important for actin-filament interactions in ADF/cofilins are structurally different in twinfilin. This explains the differences in actin-interactions (monomer versus filament binding) between twinfilin and ADF/cofilins. Taken together, our data show that the ADF-H domain is a structurally conserved actin-binding motif and that relatively small structural differences at the actin interfaces of this domain are responsible for the functional variation between the different classes of ADF-H domain proteins.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1M4J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4J OCA].
 
==Reference==
Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin., Paavilainen VO, Merckel MC, Falck S, Ojala PJ, Pohl E, Wilmanns M, Lappalainen P, J Biol Chem. 2002 Nov 8;277(45):43089-95. Epub 2002 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12207032 12207032]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Falck S]]
[[Category: Falck, S.]]
[[Category: Lappalainen P]]
[[Category: Lappalainen, P.]]
[[Category: Merckel MC]]
[[Category: Merckel, M C.]]
[[Category: Ojala PJ]]
[[Category: Ojala, P J.]]
[[Category: Paavilainen VO]]
[[Category: Paavilainen, V O.]]
[[Category: Pohl E]]
[[Category: Pohl, E.]]
[[Category: Wilmanns M]]
[[Category: Wilmanns, M.]]
[[Category: Mixed beta-sheet]]
[[Category: Pair of alpha-helice]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:37:13 2008''
Retrieved from "https://proteopedia.org/1m4j"