Publications by authors named "Omur Guven"

Tumor necrosis factor receptor-associated factors (TRAFs) are a protein family with a wide variety of roles and binding partners. Among them, TRAF6, a ubiquitin ligase, possesses unique receptor binding specificity and shows diverse functions in immune system regulation, cellular signaling, central nervous system, and tumor formation. TRAF6 consists of an N-terminal Really Interesting New Gene (RING) domain, multiple zinc fingers, and a C-terminal TRAF domain.

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X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g.

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High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Serial crystallography is an emerging structural biology technique which has fundamental limitations due to either sample volume requirements or immediate access to the competitive X-ray beamtime. Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography.

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The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach.

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Article Synopsis
  • Oligomerization of Pr55 is essential for HIV's late life cycle, and the molecule IP6 binds to the MA domain to facilitate this process, but its binding site and interaction details were previously unclear.
  • The study presents three high-resolution crystal structures showing how IP6 interacts with the MA domain, revealing key residues involved in this binding and providing new insights into HIV-1 virion assembly.
  • The findings suggest that IP6 and another molecule, PIP2, can bind simultaneously in a critical region, which plays a significant role in the localization of virion particles to the membrane during their assembly and budding.
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