Wiskott-Aldrich Syndrome protein
| Wiskott-Aldrich Syndrome protein | ||
|---|---|---|
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| other names |
WASp |
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Existing structure data : 1CEE , 1EJ5 , 1T84 , 2A3Z , 2K42 , 2OT0 |
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| Properties of human protein | ||
| Mass / length primary structure | 52.9 kDa / 502 amino acids | |
| Identifier | ||
| Gene names | WHAT IMD2 | |
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 7454 | 22376 |
| Ensemble | ENSG00000015285 | ENSMUSG00000031165 |
| UniProt | P42768 | P70315 |
| Refseq (mRNA) | NM_000377 | NM_009515 |
| Refseq (protein) | NP_000368 | NP_033541 |
| Gene locus | Chr X: 48.68 - 48.69 Mb | Chr X: 8.08 - 8.09 Mb |
| PubMed search | 7454 |
22376
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The Wiskott-Aldrich syndrome protein , abbreviated to WASp or WASP, is a regulatory protein of the WASP / WAVE protein family that is encoded by the WAS gene on the X chromosome of humans . It is an effector protein for various Rho-GTPases and activates the Arp 2/3 complex , so that it is particularly important for the polymerization of actin filaments . Mutations in the gene coding for the protein can lead to Wiskott-Aldrich syndrome , after which the protein is named.
Structure and function
The protein is responsible for signal transduction from receptors on the cell surface to the actin cytoskeleton and activates the Arp 2/3 complex, which is important for the formation of actin filaments . It is believed that the protein itself is activated by many different stimuli and can interact with other proteins. The reason for this is the many different domains that the protein has.
WASP has a GTPase-binding region that interacts with CDC42 . This GTPase-binding region can have an autoinhibitory character for the protein if it is induced by the C-terminal region or other organic molecules. Here, amino acid residues of the C-terminus, which are necessary for the activation of the Arp 2/3 complex, are blocked by interactions with the GTPase-binding region. If CDC42 now binds to the protein, changes in the conformation occur , so that the C-terminus is ultimately free and the interaction with the Arp 2/3 complex can take place.