5N74
Microtubule end binding protein complex
Summary for 5N74
| Entry DOI | 10.2210/pdb5n74/pdb |
| Descriptor | Microtubule-associated protein RP/EB family member 1, Karyogamy protein KAR9 (3 entities in total) |
| Functional Keywords | microtubule end binding protein complex, microtubule binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 16 |
| Total formula weight | 73699.69 |
| Authors | Kumar, A.,Steinmetz, M. (deposition date: 2017-02-18, release date: 2017-06-14, Last modification date: 2024-01-17) |
| Primary citation | Kumar, A.,Manatschal, C.,Rai, A.,Grigoriev, I.,Degen, M.S.,Jaussi, R.,Kretzschmar, I.,Prota, A.E.,Volkmer, R.,Kammerer, R.A.,Akhmanova, A.,Steinmetz, M.O. Short Linear Sequence Motif LxxPTPh Targets Diverse Proteins to Growing Microtubule Ends. Structure, 25:924-932.e4, 2017 Cited by PubMed Abstract: 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. PubMed: 28552577DOI: 10.1016/j.str.2017.04.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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