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.


3daw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:06, 1 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Structure of the actin-depolymerizing factor homology domain in complex with actin==
==Structure of the actin-depolymerizing factor homology domain in complex with actin==
-
<StructureSection load='3daw' size='340' side='right' caption='[[3daw]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
+
<StructureSection load='3daw' size='340' side='right'caption='[[3daw]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3daw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DAW FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3daw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DAW FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.55&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a42|2a42]], [[2hd7|2hd7]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Twf1 ([http://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=3daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3daw OCA], [https://pdbe.org/3daw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3daw RCSB], [https://www.ebi.ac.uk/pdbsum/3daw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3daw ProSAT]</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=3daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3daw OCA], [http://pdbe.org/3daw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3daw RCSB], [http://www.ebi.ac.uk/pdbsum/3daw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3daw ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://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>
+
[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 32: Line 31:
==See Also==
==See Also==
-
*[[Actin|Actin]]
+
*[[Actin 3D structures|Actin 3D structures]]
 +
*[[Twinfilin|Twinfilin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Large Structures]]
 +
[[Category: Mus musculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Goldman, A]]
+
[[Category: Goldman A]]
-
[[Category: Lappalainen, P]]
+
[[Category: Lappalainen P]]
-
[[Category: Oksanen, E]]
+
[[Category: Oksanen E]]
-
[[Category: Paavilainen, V O]]
+
[[Category: Paavilainen VO]]
-
[[Category: Actin binding protein]]
+
-
[[Category: Actin depolymerisation]]
+
-
[[Category: Cytoskeleton]]
+
-
[[Category: Structural protein-contractile protein complex]]
+
-
[[Category: Structural protein-structural protein regulator complex]]
+

Current revision

Structure of the actin-depolymerizing factor homology domain in complex with actin

PDB ID 3daw

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/3daw"
Personal tools