5n74 | pdb_00005n74

Microtubule end binding protein complex

spinqualitylabelsall models 5n74, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n74 is a 16 chain structure with sequence from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H0XPX6_OTOGA Publication Abstract from PubMed Microtubule plus-end tracking proteins (+TIPs) are involved in virtually all microtubule-based processes. End-binding (EB) proteins are considered master regulators of +TIP interaction networks, since they autonomously track growing microtubule ends and recruit a plethora of proteins to this location. Two major EB-interacting elements have been described: CAP-Gly domains and linear SxIP sequence motifs. Here, we identified LxxPTPh as a third EB-binding motif that enables major +TIPs to interact with EBs at microtubule ends. In contrast to EB-SxIP and EB-CAP-Gly, the EB-LxxPTPh binding mode does not depend on the C-terminal tail region of EB. Our study reveals that +TIPs developed additional strategies besides CAP-Gly and SxIP to target EBs at growing microtubule ends. They further provide a unique basis to discover novel +TIPs, and to dissect the role of key interaction nodes and their differential regulation for hierarchical +TIP network organization and function in eukaryotic organisms. Short Linear Sequence Motif LxxPTPh Targets Diverse Proteins to Growing Microtubule Ends.,Kumar A, Manatschal C, Rai A, Grigoriev I, Degen MS, Jaussi R, Kretzschmar I, Prota AE, Volkmer R, Kammerer RA, Akhmanova A, Steinmetz MO Structure. 2017 Jun 6;25(6):924-932.e4. doi: 10.1016/j.str.2017.04.010. Epub 2017, May 25. PMID:28552577 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also End-binding protein

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