9f07

TUBULIN:STATHMIN:DARPIN:TAU MTBR3 COMPLEXTUBULIN:STATHMIN:DARPIN:TAU MTBR3 COMPLEX

Structural highlights 9f07 is a 8 chain structure with sequence from Homo sapiens, Ovis aries and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.211Å Ligands: , , , , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0VWZ0_SHEEP Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] Publication Abstract from PubMed Tau is a protein involved in the regulation of axonal microtubules in neurons. In pathological conditions, it forms filamentous aggregates which are molecular markers of neurodegenerative diseases known as tauopathies. Structures of Tau in fibrils or bound to the microtubule have been reported. We present here a structure of a Tau construct comprising the PHF6 motif, an oligopeptide involved in Tau aggregation, as a complex with tubulin. This Tau fragment binds as a dimer to a new site which, when transposed to the microtubule, would correspond to a pore between protofilaments. These results raise new hypotheses on Tau-induced microtubule assembly and stabilization and on Tau oligomerization. The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.,Ammar Khodja L, Campanacci V, Lippens G, Gigant B PNAS Nexus. 2024 Oct 30;3(11):pgae487. doi: 10.1093/pnasnexus/pgae487. , eCollection 2024 Nov. PMID:39534653 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 9f07, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image