Wiskott-Aldrich syndrome protein

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<StructureSection load='2a3z' size='340' side='right' caption='Human WASP WH2 domain (pink) complex with α-actin (grey), DNAse I (green), ATP, Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code [[2a3z]])' scene='70/706797/Cv/1'>
<StructureSection load='2a3z' size='340' side='right' caption='Human WASP WH2 domain (pink) complex with α-actin (grey), DNAse I (green), ATP, Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code [[2a3z]])' scene='70/706797/Cv/1'>
== Function ==
== Function ==
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'''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<ref>PMID:22411869</ref>.
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'''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.
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*'''N-WASP''' (Neural WASP) belongs to the WASP family of proteins. Human N-WASP stimulates the actin-nucleating activity<ref>PMID:22411869</ref>.
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*'''WAVE-1''' facilitates neuronal actin remodeling<ref>PMID:17215396</ref>.
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*'''WAVE-2''' facilitates cytoskeletal actin remodeling<ref>PMID:16401421</ref>.
== Relevance ==
== Relevance ==
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Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune disregulation<ref>PMID:18043243</ref>.
Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune disregulation<ref>PMID:18043243</ref>.
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</StructureSection>
 
== 3D Structures of Wiskott-Aldrich syndrome protein ==
== 3D Structures of Wiskott-Aldrich syndrome protein ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[Wiskott-Aldrich syndrome protein 3D structures]]
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*WASP; Domains - CRIB 242-310; WH2 430-458
 
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**[[1ej5]] – hWASP CRIB domain + 461-492 autoinhibited – human - NMR<br />
 
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**[[1t84]] – hWASP CRIB domain + 461-492 autoinhibited + wiskostatin - NMR<br />
 
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**[[1cee]] – hWASP CRIB domain + CDC42 - NMR<br />
 
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**[[2a3z]] – hWASP WH2 domain + α-actin + DNAse I + ATP<br />
 
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**[[2ot0]] – hWASP C terminal + fructose-bisphosphate aldolase<br />
 
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**[[2k42]] – hWASP CRIB domain + ESPFU - NMR<br />
 
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**[[3p8c]] – hWASP + SRA1 + NAP 1 + BRICK1 + ABL interactor <br />
 
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**[[4n78]] – hWASP + SRA1 + NAP 1 + BRICK1 + WIRS + ABL interactor <br />
 
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*Neural WASP
 
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**[[1mke]], [[2ifs]] – hWASP EVH1 domain 26-147/rWIP 461-485 - NMR<br />
 
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**[[2ff3]] – hWASP WH2-2 domain + α-actin + gelsolin domain 1<br />
 
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**[[2vcp]] – hWASP WH2-1,2,C domain 392-484 + α-actin<br />
 
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**[[2lnh]] – hWASP CRIB + ESPFU + insulin receptor tyrosine kinase substrate - NMR<br />
 
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**[[3m3n]] – mWASP tandem W domain 397-444 + α-actin - mouse<br />
 
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**[[6uhc]] – mWASP in ARP2/3 complex – Cryo EM<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

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