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.


2a41

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2a41.gif|left|200px]]
[[Image:2a41.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2a41 |SIZE=350|CAPTION= <scene name='initialview01'>2a41</scene>, resolution 2.60&Aring;
+
The line below this paragraph, containing "STRUCTURE_2a41", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <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>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2a41| PDB=2a41 | SCENE= }}
-
|RELATEDENTRY=[[2a3z|2A3Z]], [[2a40|2A40]], [[2a42|2A42]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a41 OCA], [http://www.ebi.ac.uk/pdbsum/2a41 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a41 RCSB]</span>
+
-
}}
+
'''Ternary complex of the WH2 Domain of WIP with Actin-DNAse I'''
'''Ternary complex of the WH2 Domain of WIP with Actin-DNAse I'''
Line 30: Line 27:
[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
[[Category: Kerff, F.]]
[[Category: Kerff, F.]]
-
[[Category: actin]]
+
[[Category: Actin]]
-
[[Category: arp2/3]]
+
[[Category: Arp2/3]]
-
[[Category: dnase i]]
+
[[Category: Dnase i]]
-
[[Category: wasp]]
+
[[Category: Wasp]]
-
[[Category: wh2]]
+
[[Category: Wh2]]
-
[[Category: wip]]
+
[[Category: Wip]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:34:35 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:47:34 2008''
+

Revision as of 15:34, 3 May 2008

Image:2a41.gif

Template:STRUCTURE 2a41

Ternary complex of the WH2 Domain of WIP with Actin-DNAse I


Overview

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) is a small and widespread actin-binding motif. In the WASP family, WH2 plays a role in filament nucleation by Arp2/3 complex. Here we describe the crystal structures of complexes of actin with the WH2 domains of WASP, WASP-family verprolin homologous protein, and WASP-interacting protein. Despite low sequence identity, WH2 shares structural similarity with the N-terminal portion of the actin monomer-sequestering thymosin beta domain (Tbeta). We show that both domains inhibit nucleotide exchange by targeting the cleft between actin subdomains 1 and 3, a common binding site for many unrelated actin-binding proteins. Importantly, WH2 is significantly shorter than Tbeta but binds actin with approximately 10-fold higher affinity. WH2 lacks a C-terminal extension that in Tbeta4 becomes involved in monomer sequestration by interfering with intersubunit contacts in F-actin. Owing to their shorter length, WH2 domains connected in tandem by short linkers can coexist with intersubunit contacts in F-actin and are proposed to function in filament nucleation by lining up actin subunits along a filament strand. The WH2-central region of WASP-family proteins is proposed to function in an analogous way by forming a special class of tandem repeats whose function is to line up actin and Arp2 during Arp2/3 nucleation. The structures also suggest a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH2, thereby playing a role in filament elongation.

About this Structure

2A41 is a Protein complex structure of sequences from Bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly., Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez R, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16644-9. Epub 2005 Nov 7. PMID:16275905 Page seeded by OCA on Sat May 3 18:34:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a41"
Personal tools