3E2U
Crystal structure of the zink-knuckle 2 domain of human CLIP-170 in complex with CAP-Gly domain of human dynactin-1 (p150-GLUED)
Replaces: 2PZOSummary for 3E2U
Entry DOI | 10.2210/pdb3e2u/pdb |
Related | 1TXQ 2CP5 2HKN 2HKQ 2HQH |
Descriptor | Dynactin subunit 1, CAP-Gly domain-containing linker protein 1, ZINC ION, ... (4 entities in total) |
Functional Keywords | structural protein microtubule binding, dynactin, cytoskeleton associated protein, p150glued, clip-170/restin, +tip protein complex structure, zinc-knuckle, autoinhibition, protein binding, cytoskeleton, dynein, microtubule, motor protein, phosphoprotein |
Biological source | Homo sapiens (Human) More |
Cellular location | Cytoplasm: Q14203 P30622 |
Total number of polymer chains | 8 |
Total formula weight | 60715.70 |
Authors | Weisbrich, A.,Honnappa, S.,Capitani, G.,Steinmetz, M.O. (deposition date: 2008-08-06, release date: 2008-08-19, Last modification date: 2023-11-01) |
Primary citation | Weisbrich, A.,Honnappa, S.,Jaussi, R.,Okhrimenko, O.,Frey, D.,Jelesarov, I.,Akhmanova, A.,Steinmetz, M.O. Structure-function relationship of CAP-Gly domains Nat.Struct.Mol.Biol., 14:959-967, 2007 Cited by PubMed Abstract: In all eukaryotes, CAP-Gly proteins control important cellular processes. The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle of CLIP170 as a model system to explore the structure-function relationship of CAP-Gly-mediated protein interactions. We demonstrate that the conserved GKNDG motif of CAP-Gly domains is responsible for targeting to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and microtubules. The CAP-Gly-EEY/F interaction is essential for the recruitment of the dynactin complex by CLIP170 and for activation of CLIP170. Our findings define the molecular basis of CAP-Gly domain function, including the tubulin detyrosination-tyrosination cycle. They further establish fundamental roles for the interaction between CAP-Gly proteins and C-terminal EEY/F sequence motifs in regulating complex and dynamic cellular processes. PubMed: 17828277DOI: 10.1038/nsmb1291 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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