6kip

Crystal structure of PTPRD phosphatase domain in complex with Liprin-alpha3 tandem SAM domains

spinqualitylabelsall models 6kip, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kip is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.911Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTPRD_MOUSE Publication Abstract from PubMed Synapse formation is induced by transsynaptic interaction of neuronal cell-adhesion molecules termed synaptic organizers. Type IIa receptor protein tyrosine phosphatases (IIa RPTPs) function as presynaptic organizers. The cytoplasmic domain of IIa RPTPs consists of two phosphatase domains, and the membrane-distal one (D2) is essential for synapse formation. Liprin-alpha, which is an active zone protein critical for synapse formation, interacts with D2 via its C-terminal domain composed of three tandem sterile alpha motifs (tSAM). Structural mechanisms of this critical interaction for synapse formation remain elusive. Here, we report the crystal structure of the complex between mouse PTPdelta D2 and Liprin-alpha3 tSAM at 1.91 A resolution. PTPdelta D2 interacts with the N-terminal helix and the first and second SAMs (SAM1 and SAM2, respectively) of Liprin-alpha3. Structure-based mutational analyses in vitro and in cellulo demonstrate that the interactions with Liprin-alpha SAM1 and SAM2 are essential for the binding and synaptogenic activity. Structural insights into selective interaction between type IIa receptor protein tyrosine phosphatases and Liprin-alpha.,Wakita M, Yamagata A, Shiroshima T, Izumi H, Maeda A, Sendo M, Imai A, Kubota K, Goto-Ito S, Sato Y, Mori H, Yoshida T, Fukai S Nat Commun. 2020 Jan 31;11(1):649. doi: 10.1038/s41467-020-14516-5. PMID:32005855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase 3D structures

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