Wiskott-Aldrich syndrome protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<StructureSection load='2a3z' size='340' side='right' caption='Human WASP WH2 domain (pink) complex with α-actin (grey), DNAse I (green), ATP (stick model), Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code [[2a3z]])' scene=''>
<StructureSection load='2a3z' size='340' side='right' caption='Human WASP WH2 domain (pink) complex with α-actin (grey), DNAse I (green), ATP (stick model), Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code [[2a3z]])' scene=''>
-
'''Wiskott-Aldrich syndrome protein''' (WASP) is involved in nucleating of new F-actin. In the autoinhibited form of WASP a region of the N-terminal interacts with a region of its C-terminal. This interaction is disrupted by CDC42 and phosphatidylinositol 4,5-bisphosphate (PIP2) resulting in the active WASP. '''N-WASP''' (Neural WASP) belongs to the WASP family of proteins. Human N-WASP stimulates the actin-nucleating activity. N-WASP induces actin polymerization in the Shigella bacterium. This bacterium causes dysentery.
+
'''Wiskott-Aldrich syndrome protein''' (WASP) is involved in nucleating of new F-actin. In the autoinhibited form of WASP a region of the N-terminal interacts with a region of its C-terminal. This interaction is disrupted by CDC42 and phosphatidylinositol 4,5-bisphosphate (PIP2) resulting in the active WASP. WASP domains include '''EVH1''' domain in the N-terminal which bind proline-rich sequences in the WASP-interacting proteins; '''WH2''' domain is ca. 18 residues long and interacts with actin; '''CRIB or GTPase-binding''' domain which interacts with CDC42. '''N-WASP''' (Neural WASP) belongs to the WASP family of proteins. Human N-WASP stimulates the actin-nucleating activity. N-WASP induces actin polymerization in the Shigella bacterium. This bacterium causes dysentery.
== Function ==
== Function ==
Line 23: Line 23:
**[[1ej5]] – hWASP autoinhibited – human - NMR<br />
**[[1ej5]] – hWASP autoinhibited – human - NMR<br />
**[[1t84]] – hWASP autoinhibited + wiskostatin - NMR<br />
**[[1t84]] – hWASP autoinhibited + wiskostatin - NMR<br />
-
**[[1cee]] – hWASP GTPase binding domain + CDC42 - NMR<br />
+
**[[1cee]] – hWASP CRIB domain + CDC42 - NMR<br />
**[[2a3z]] – hWASP WH2 domain + α-actin + DNAse I + ATP<br />
**[[2a3z]] – hWASP WH2 domain + α-actin + DNAse I + ATP<br />
**[[2ot0]] – hWASP C terminal + fructose-bisphosphate aldolase<br />
**[[2ot0]] – hWASP C terminal + fructose-bisphosphate aldolase<br />
Line 33: Line 33:
**[[2ff3]] – hWASP WH2-2 domain + α-actin + gelsolin domain 1<br />
**[[2ff3]] – hWASP WH2-2 domain + α-actin + gelsolin domain 1<br />
**[[2vcp]] – hWASP WH2-1,2,C domain + α-actin<br />
**[[2vcp]] – hWASP WH2-1,2,C domain + α-actin<br />
-
**[[2lnh]] – hWASP residues 207-270 + ESPFU + insulin receptor tyrosine kinase substrate - NMR<br />
+
**[[2lnh]] – hWASP CRIB + ESPFU + insulin receptor tyrosine kinase substrate - NMR<br />
**[[3m3n]] – WASP tandem W domain + α-actin - mouse<br />
**[[3m3n]] – WASP tandem W domain + α-actin - mouse<br />
}}
}}
== References ==
== References ==
<references/>
<references/>

Revision as of 10:23, 15 July 2015

Human WASP WH2 domain (pink) complex with α-actin (grey), DNAse I (green), ATP (stick model), Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code 2a3z)

Drag the structure with the mouse to rotate

3D Structures of Wiskott-Aldrich syndrome protein

Updated on 15-July-2015

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Wiskott-Aldrich_syndrome_protein"
Personal tools