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3NRX

Insights into anti-parallel microtubule crosslinking by PRC1, a conserved non-motor microtubule binding protein

Summary for 3NRX
Entry DOI10.2210/pdb3nrx/pdb
Related3NRY
DescriptorProtein regulator of cytokinesis 1 (2 entities in total)
Functional Keywordsspectrin fold, microtubule binding domain, protein binding
Biological sourceHomo sapiens (human)
Cellular locationNucleus: O43663
Total number of polymer chains2
Total formula weight31676.14
Authors
Kapoor, T.M.,Subramanian, R.,Wilson-Kubalek, E.M.,Arthur, C.P.,Bick, M.J.,Campbell, E.A.,Darst, S.A.,Milligan, R.A. (deposition date: 2010-06-30, release date: 2010-08-18, Last modification date: 2023-09-06)
Primary citationSubramanian, R.,Wilson-Kubalek, E.M.,Arthur, C.P.,Bick, M.J.,Campbell, E.A.,Darst, S.A.,Milligan, R.A.,Kapoor, T.M.
Insights into Antiparallel Microtubule Crosslinking by PRC1, a Conserved Nonmotor Microtubule Binding Protein.
Cell(Cambridge,Mass.), 142:433-443, 2010
Cited by
PubMed Abstract: Formation of microtubule architectures, required for cell shape maintenance in yeast, directional cell expansion in plants and cytokinesis in eukaryotes, depends on antiparallel microtubule crosslinking by the conserved MAP65 protein family. Here, we combine structural and single molecule fluorescence methods to examine how PRC1, the human MAP65, crosslinks antiparallel microtubules. We find that PRC1's microtubule binding is mediated by a structured domain with a spectrin-fold and an unstructured Lys/Arg-rich domain. These two domains, at each end of a homodimer, are connected by a linkage that is flexible on single microtubules, but forms well-defined crossbridges between antiparallel filaments. Further, we show that PRC1 crosslinks are compliant and do not substantially resist filament sliding by motor proteins in vitro. Together, our data show how MAP65s, by combining structural flexibility and rigidity, tune microtubule associations to establish crosslinks that selectively "mark" antiparallel overlap in dynamic cytoskeletal networks.
PubMed: 20691902
DOI: 10.1016/j.cell.2010.07.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

239149

數據於2025-07-23公開中

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