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MRC Laboratory of Molecular Biology

MRC Laboratory of Molecular Biology

One of the world's leading research institutes, our scientists are working to advance understanding of biological processes at the molecular level - providing the knowledge needed to solve key problems in human health.

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Proteins required for processing the end of mRNAs identified

CryoEM structure of the polymerase module of CPF in complex with RNA, the PSR of Mpe1 and the yPIM of Cft2. The structure shows how Mpe1 (orange) directly contacts RNA (gray), and Cft2 (light blue) binds to the polymerase module of the yeast cleavage and polyadenylation factor (CPF).

Lori Passmore’s group in the LMB’s Structural Studies Division has shown that Mpe1 in yeast and RBBP6 in humans are critical for activating CPF and CPSF respectively, protein complexes vital to cleavage process of mRNA.

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Published on 17th May, 2022

Human inner kinetochore structure reveals mechanism for binding DNA during mitosis

Structure of the inner kinetochore bound to centromeric CENP-A nucleosome

In solving the structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome, David Barford’s group in the LMB’s Structural Studies Division has revealed how the complex recognises centromeric DNA and functions as a load-bearing element during chromosome segregation.

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Published on 19th April, 2022

Structural study reveals unexpected diversity in GABAA receptor assembly

GABAA receptors, which mediate essential signalling in the brain and beyond, can assemble into a much larger number of arrangements than previously anticipated. This diversity enables complex responses to both neurotransmitters and drugs. Image shows structures of GABAA receptors in variety of arrangements.

Structural analysis of GABAA receptors by Radu Aricescu’s group, in the LMB’s Neurobiology Division, has revealed possibility for an unexpected variety in subunit arrangement, with significant implications for future research and therapeutic developments.

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Published on 30th March, 2022

TMEM106B filaments form in an age-dependent manner in human brains

Inter-divisional collaboration between the groups of Sjors Scheres, Michel Goedert and others identified TMEM106B as a new protein responsible for amyloid filament formation, and showed that these filaments develop in an age-dependent manner in human brains.

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Published on 28th March, 2022

Structural study reveals a novel activation mechanism for the fungal GPCR, Ste2

Structural snapshots of the Class D GPCR dimer, Ste2 (blue, green), along its activation pathway using cryo-EM. This provides a detailed picture, revealing a fundamentally different activation mechanism to previously-known GPCRs.

Chris Tate’s group, in the LMB’s Structural Studies Division, have used cryo-EM analysis to show that Ste2, a fungal Class D GPCR, has a fundamentally distinct activation mechanism in comparison to other types of GPCRs.

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Published on 16th March, 2022

Cryo-EM structures reveal molecular basis of human telomerase recruitment

Cartoon-like image of two hands (representing TPP1 and POT1) pulling on a rope (representing DNA) to illustrate how these proteins assist telomeric DNA binding to telomerase (represented as a newly discovered cryo-EM structure).

Kelly Nguyen’s group in the LMB’s Structural Studies Division has determined the molecular basis of how the TPP1 and POT1 components of shelterin recruit human telomerase to telomeres and regulate the enzyme’s activity during genomic replication.

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Published on 25th February, 2022
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