5o2m | pdb_00005o2m

p130Cas SH3 domain

spinqualitylabelsall models 5o2m, 40 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o2m is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed CAS is a docking protein downstream of the proto-oncogene Src with a role in invasion and metastasis of cancer cells. The CAS SH3 domain is indispensable for CAS-mediated signaling, but structural aspects of CAS SH3 ligand binding and regulation are not well understood. Here, we identified the consensus CAS SH3 binding motif and structurally characterized the CAS SH3 domain in complex with ligand. We revealed the requirement for an uncommon centrally localized lysine residue at position +2 of CAS SH3 ligands and two rather dissimilar optional anchoring residues, leucine and arginine, at position +5. We further expanded the knowledge of CAS SH3 ligand binding regulation by manipulating tyrosine 12 phosphorylation and confirmed the negative role of this phosphorylation on CAS SH3 ligand binding. Finally, by exploiting the newly identified binding requirements of the CAS SH3 domain, we predicted and experimentally verified two novel CAS SH3 binding partners, DOK7 and GLIS2. Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.,Gemperle J, Hexnerova R, Lepsik M, Tesina P, Dibus M, Novotny M, Brabek J, Veverka V, Rosel D Sci Rep. 2017 Aug 14;7(1):8057. doi: 10.1038/s41598-017-08303-4. PMID:28808245 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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