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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 (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, Ca+2 and Mg+2 ions, glycerol and formic acid (PDB code [[2a3z]])' scene='70/706797/Cv/1'> |
| - | '''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>. N-WASP induces actin polymerization in the Shigella bacterium. This bacterium causes dysentery.
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| | == Function == | | == Function == |
| - | | + | '''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. |
| - | == Disease ==
| + | *'''N-WASP''' (Neural WASP) belongs to the WASP family of proteins. Human N-WASP stimulates the actin-nucleating activity<ref>PMID:22411869</ref>. |
| - | | + | *'''WAVE-1''' facilitates neuronal actin remodeling<ref>PMID:17215396</ref>. |
| - | Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune dysregulation<ref>PMID:18043243</ref>.
| + | *'''WAVE-2''' facilitates cytoskeletal actin remodeling<ref>PMID:16401421</ref>. |
| | | | |
| | == Relevance == | | == Relevance == |
| | + | N-WASP induces actin polymerization in the ''Shigella'' bacterium<ref>PMID:11952639</ref>. This bacterium causes dysentery. |
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| - | == Structural highlights == | + | == Disease == |
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| - | </StructureSection> | + | Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune disregulation<ref>PMID:18043243</ref>. |
| | | | |
| | == 3D Structures of Wiskott-Aldrich syndrome protein == | | == 3D Structures of Wiskott-Aldrich syndrome protein == |
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| + | [[Wiskott-Aldrich syndrome protein 3D structures]] |
| - | {{#tree:id=OrganizedByTopic|openlevels=0|
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| - | *WASP | |
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| - | **[[1ej5]] – hWASP autoinhibited – human - NMR<br /> | |
| - | **[[1t84]] – hWASP autoinhibited + wiskostatin - NMR<br /> | |
| - | **[[1cee]] – hWASP CRIB domain + CDC42 - NMR<br /> | |
| - | **[[2a3z]] – hWASP WH2 domain + α-actin + DNAse I + ATP<br /> | |
| - | **[[2ot0]] – hWASP C terminal + fructose-bisphosphate aldolase<br /> | |
| - | **[[2k42]] – hWASP CRIB domain + ESPFU - NMR<br /> | |
| - | | |
| - | *N-WASP | |
| - | | |
| - | **[[1mke]], [[2ifs]] – hWASP EVH1 domain/WIP peptide - NMR<br /> | |
| - | **[[2ff3]] – hWASP WH2-2 domain + α-actin + gelsolin domain 1<br /> | |
| - | **[[2vcp]] – hWASP WH2-1,2,C domain + α-actin<br /> | |
| - | **[[2lnh]] – hWASP CRIB + ESPFU + insulin receptor tyrosine kinase substrate - NMR<br /> | |
| - | **[[3m3n]] – WASP tandem W domain + α-actin - mouse<br /> | |
| - | }} | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | + | </StructureSection> |
| | + | [[Category:Topic Page]] |
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Function
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[1].
- WAVE-1 facilitates neuronal actin remodeling[2].
- WAVE-2 facilitates cytoskeletal actin remodeling[3].
Relevance
N-WASP induces actin polymerization in the Shigella bacterium[4]. This bacterium causes dysentery.
Disease
Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune disregulation[5].
3D Structures of Wiskott-Aldrich syndrome protein
Wiskott-Aldrich syndrome protein 3D structures
References
- ↑ Westerberg LS, Dahlberg C, Baptista M, Moran CJ, Detre C, Keszei M, Eston MA, Alt FW, Terhorst C, Notarangelo LD, Snapper SB. Wiskott-Aldrich syndrome protein (WASP) and N-WASP are critical for peripheral B-cell development and function. Blood. 2012 Apr 26;119(17):3966-74. doi: 10.1182/blood-2010-09-308197. Epub 2012 , Mar 12. PMID:22411869 doi:http://dx.doi.org/10.1182/blood-2010-09-308197
- ↑ Soderling SH, Guire ES, Kaech S, White J, Zhang F, Schutz K, Langeberg LK, Banker G, Raber J, Scott JD. A WAVE-1 and WRP signaling complex regulates spine density, synaptic plasticity, and memory. J Neurosci. 2007 Jan 10;27(2):355-65. PMID:17215396 doi:10.1523/JNEUROSCI.3209-06.2006
- ↑ Nolz JC, Gomez TS, Zhu P, Li S, Medeiros RB, Shimizu Y, Burkhardt JK, Freedman BD, Billadeau DD. The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation. Curr Biol. 2006 Jan 10;16(1):24-34. PMID:16401421 doi:10.1016/j.cub.2005.11.036
- ↑ Suzuki T, Mimuro H, Suetsugu S, Miki H, Takenawa T, Sasakawa C. Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading. Cell Microbiol. 2002 Apr;4(4):223-33. PMID:11952639
- ↑ Notarangelo LD, Miao CH, Ochs HD. Wiskott-Aldrich syndrome. Curr Opin Hematol. 2008 Jan;15(1):30-6. PMID:18043243 doi:http://dx.doi.org/10.1097/MOH.0b013e3282f30448
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