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( A ) Cartoon representation of the asymmetric unit of the crystal structure of Aurora-A M7KD bound to CEP19 468-533 and the inhibitory <t>monobody.</t> There are two copies of Aurora-A M7KD (Chain A in light green, Chain D in light pink), 2 copies of the inhibitory monobody (Chains B and E in cyan) and 2 copies of CEP192 468-533 (Chains C and F in blue and dark blue). Only part of the CEP192 was visible in chain F (residues 506–526). ( B ) Overlay of the cartoon representations of the two Aurora-A M7KD copies in the asymmetric unit. Chain A is shown in light green, with chain D in light pink. There are no significant differences between the two copies in the asymmetric unit. ( C ) Cartoon representation of the complex between CEP192 468-533_C (dark blue) and Aurora-A M7KD_A (light green) with a symmetry-related copy Mb2 (teal). The interface was analysed on PDBePISA, giving an interface score of 0.00 suggesting that this is merely a crystal contact and not a biologically relevant interface. ( D ) Representation of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green). The mesh represents a 2mFo-DFc map contoured at 1.2σ. ( E ) A second view of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green) to show the αS/αL region. The mesh represents a 2mFo-DFc map contoured at 1.2σ. Data information: Regions modelled for the different chains were 124–275 and 289–389 (chain A, Aurora-A M7KD ); 3–93 (chain B, Mb2); 468–531 (chain C, CEP192 468_533 ); 126–277 and 290–388 (chain D, Aurora-A M7KD ); 3–93 (chain E, Mb2); 506–527 (chain F, CEP192 468_533 ).
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( A ) Cartoon representation of the asymmetric unit of the crystal structure of Aurora-A M7KD bound to CEP19 468-533 and the inhibitory <t>monobody.</t> There are two copies of Aurora-A M7KD (Chain A in light green, Chain D in light pink), 2 copies of the inhibitory monobody (Chains B and E in cyan) and 2 copies of CEP192 468-533 (Chains C and F in blue and dark blue). Only part of the CEP192 was visible in chain F (residues 506–526). ( B ) Overlay of the cartoon representations of the two Aurora-A M7KD copies in the asymmetric unit. Chain A is shown in light green, with chain D in light pink. There are no significant differences between the two copies in the asymmetric unit. ( C ) Cartoon representation of the complex between CEP192 468-533_C (dark blue) and Aurora-A M7KD_A (light green) with a symmetry-related copy Mb2 (teal). The interface was analysed on PDBePISA, giving an interface score of 0.00 suggesting that this is merely a crystal contact and not a biologically relevant interface. ( D ) Representation of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green). The mesh represents a 2mFo-DFc map contoured at 1.2σ. ( E ) A second view of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green) to show the αS/αL region. The mesh represents a 2mFo-DFc map contoured at 1.2σ. Data information: Regions modelled for the different chains were 124–275 and 289–389 (chain A, Aurora-A M7KD ); 3–93 (chain B, Mb2); 468–531 (chain C, CEP192 468_533 ); 126–277 and 290–388 (chain D, Aurora-A M7KD ); 3–93 (chain E, Mb2); 506–527 (chain F, CEP192 468_533 ).
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( A ) Cartoon representation of the asymmetric unit of the crystal structure of Aurora-A M7KD bound to CEP19 468-533 and the inhibitory <t>monobody.</t> There are two copies of Aurora-A M7KD (Chain A in light green, Chain D in light pink), 2 copies of the inhibitory monobody (Chains B and E in cyan) and 2 copies of CEP192 468-533 (Chains C and F in blue and dark blue). Only part of the CEP192 was visible in chain F (residues 506–526). ( B ) Overlay of the cartoon representations of the two Aurora-A M7KD copies in the asymmetric unit. Chain A is shown in light green, with chain D in light pink. There are no significant differences between the two copies in the asymmetric unit. ( C ) Cartoon representation of the complex between CEP192 468-533_C (dark blue) and Aurora-A M7KD_A (light green) with a symmetry-related copy Mb2 (teal). The interface was analysed on PDBePISA, giving an interface score of 0.00 suggesting that this is merely a crystal contact and not a biologically relevant interface. ( D ) Representation of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green). The mesh represents a 2mFo-DFc map contoured at 1.2σ. ( E ) A second view of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green) to show the αS/αL region. The mesh represents a 2mFo-DFc map contoured at 1.2σ. Data information: Regions modelled for the different chains were 124–275 and 289–389 (chain A, Aurora-A M7KD ); 3–93 (chain B, Mb2); 468–531 (chain C, CEP192 468_533 ); 126–277 and 290–388 (chain D, Aurora-A M7KD ); 3–93 (chain E, Mb2); 506–527 (chain F, CEP192 468_533 ).
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Image Search Results


( A ) Cartoon representation of the asymmetric unit of the crystal structure of Aurora-A M7KD bound to CEP19 468-533 and the inhibitory monobody. There are two copies of Aurora-A M7KD (Chain A in light green, Chain D in light pink), 2 copies of the inhibitory monobody (Chains B and E in cyan) and 2 copies of CEP192 468-533 (Chains C and F in blue and dark blue). Only part of the CEP192 was visible in chain F (residues 506–526). ( B ) Overlay of the cartoon representations of the two Aurora-A M7KD copies in the asymmetric unit. Chain A is shown in light green, with chain D in light pink. There are no significant differences between the two copies in the asymmetric unit. ( C ) Cartoon representation of the complex between CEP192 468-533_C (dark blue) and Aurora-A M7KD_A (light green) with a symmetry-related copy Mb2 (teal). The interface was analysed on PDBePISA, giving an interface score of 0.00 suggesting that this is merely a crystal contact and not a biologically relevant interface. ( D ) Representation of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green). The mesh represents a 2mFo-DFc map contoured at 1.2σ. ( E ) A second view of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green) to show the αS/αL region. The mesh represents a 2mFo-DFc map contoured at 1.2σ. Data information: Regions modelled for the different chains were 124–275 and 289–389 (chain A, Aurora-A M7KD ); 3–93 (chain B, Mb2); 468–531 (chain C, CEP192 468_533 ); 126–277 and 290–388 (chain D, Aurora-A M7KD ); 3–93 (chain E, Mb2); 506–527 (chain F, CEP192 468_533 ).

Journal: The EMBO Journal

Article Title: CEP192 localises mitotic Aurora-A activity by priming its interaction with TPX2

doi: 10.1038/s44318-024-00240-z

Figure Lengend Snippet: ( A ) Cartoon representation of the asymmetric unit of the crystal structure of Aurora-A M7KD bound to CEP19 468-533 and the inhibitory monobody. There are two copies of Aurora-A M7KD (Chain A in light green, Chain D in light pink), 2 copies of the inhibitory monobody (Chains B and E in cyan) and 2 copies of CEP192 468-533 (Chains C and F in blue and dark blue). Only part of the CEP192 was visible in chain F (residues 506–526). ( B ) Overlay of the cartoon representations of the two Aurora-A M7KD copies in the asymmetric unit. Chain A is shown in light green, with chain D in light pink. There are no significant differences between the two copies in the asymmetric unit. ( C ) Cartoon representation of the complex between CEP192 468-533_C (dark blue) and Aurora-A M7KD_A (light green) with a symmetry-related copy Mb2 (teal). The interface was analysed on PDBePISA, giving an interface score of 0.00 suggesting that this is merely a crystal contact and not a biologically relevant interface. ( D ) Representation of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green). The mesh represents a 2mFo-DFc map contoured at 1.2σ. ( E ) A second view of the electron density around CEP192 468-533 (dark blue) when bound to Aurora-A M7KD (light green) to show the αS/αL region. The mesh represents a 2mFo-DFc map contoured at 1.2σ. Data information: Regions modelled for the different chains were 124–275 and 289–389 (chain A, Aurora-A M7KD ); 3–93 (chain B, Mb2); 468–531 (chain C, CEP192 468_533 ); 126–277 and 290–388 (chain D, Aurora-A M7KD ); 3–93 (chain E, Mb2); 506–527 (chain F, CEP192 468_533 ).

Article Snippet: A codon-optimised construct encoding human CEP192 1-1000 with an N-terminal GST tag and the inhibitory monobody with an N-terminal Hexa-His-SUMO tag (Mb2) were obtained from GenScript (Zorba et al, ).

Techniques:

Reagents and tools table

Journal: The EMBO Journal

Article Title: CEP192 localises mitotic Aurora-A activity by priming its interaction with TPX2

doi: 10.1038/s44318-024-00240-z

Figure Lengend Snippet: Reagents and tools table

Article Snippet: A codon-optimised construct encoding human CEP192 1-1000 with an N-terminal GST tag and the inhibitory monobody with an N-terminal Hexa-His-SUMO tag (Mb2) were obtained from GenScript (Zorba et al, ).

Techniques: Recombinant, Plasmid Preparation, Sequencing, CRISPR, Control, Protease Inhibitor, Transfection, Software, Protein Purification, Mutagenesis, Mass Spectrometry, Western Blot