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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural requirements for the specific binding of CRABP2 to cyclin D3 Martyna W. Pastok , Charles W. E. Tomlinson , Shannon Turberville , Abbey M. Butler , Arnaud Basle , Martin E. M. Noble , Jane A. Endicott , Ehmke Pohl , Natalie J. Tatum Structure 173 DOI: 10.1016/j.str.2024.09.020 Diamond Proposal Number(s): [18598] Open Access Show Abstract ▼ Abstract: Cellular retinoic acid binding protein 2 (CRABP2) transports retinoic acid from the cytoplasm to the nucleus where it then transfers its cargo to retinoic acid receptor-containing complexes leading to activation of gene transcription. We demonstrate using purified proteins that CRABP2 is also a cyclin D3-specific binding protein and that the CRABP2 cyclin D3 binding site and the proposed CRABP2 nuclear localization sequence overlap. Both sequences are within the helix-loop-helix motif that forms a lid to the retinoic acid binding pocket. Mutations within this sequence that block both cyclin D3 and retinoic acid binding promote formation of a CRABP2 structure in which the retinoic acid binding pocket is occupied by an alternative lid conformation. Structural and functional analysis of CRABP2 and cyclin D3 mutants combined with AlphaFold models of the ternary CDK4/6-cyclin D3-CRABP2 complex supports the identification of an α-helical protein binding site on the cyclin D3 C-terminal cyclin box fold.	Oct 2024
B21-High Throughput SAXS I04-1-Macromolecular Crystallography (fixed wavelength)	Discriminative SKP2 interactions with CDK-cyclin complexes support a cyclin a-specific role in p27KIP1 degradation Marco Salamina , Bailey C. Montefiore , Mengxi Liu , Daniel J. Wood , Richard Heath , James R. Ault , Lan-Zhen Wang , Svitlana Korolchuk , Arnaud Basle , Martyna Pastok , Judith Reeks , Natalie J. Tatum , Frank Sobott , Stefan T. Arold , Michele Pagano , Martin E. M. Noble , Jane A. Endicott Journal Of Molecular Biology 433 DOI: 10.1016/j.jmb.2020.166795 Diamond Proposal Number(s): [13587, 16970] Open Access Show Abstract ▼ Abstract: The SCFSKP2 ubiquitin ligase relieves G1 checkpoint control of CDK-cyclin complexes by promoting p27KIP1 degradation. We describe reconstitution of stable complexes containing SKP1-SKP2 and CDK1-cyclin B or CDK2-cyclin A/E, mediated by the CDK regulatory subunit CKS1. We further show that a direct interaction between a SKP2 N-terminal motif and cyclin A can stabilize SKP1-SKP2-CDK2-cyclin A complexes in the absence of CKS1. We identify the SKP2 binding site on cyclin A and demonstrate the site is not present in cyclin B or cyclin E. This site is distinct from but overlapping with features that mediate binding of p27KIP1 and other G1 cyclin regulators to cyclin A. We propose that the capacity of SKP2 to engage with CDK2-cyclin A by more than one structural mechanism provides a way to fine tune the degradation of p27KIP1 and distinguishes cyclin A from other G1 cyclins to ensure orderly cell cycle progression.	Mar 2021

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