Results 81 to 90 of about 10,740 (213)
Visualization of allostery in P-selectin lectin domain using MD simulations.
Allostery of P-selectin lectin (Lec) domain followed by an epithelial growth factor (EGF)-like domain is essential for its biological functionality, but the underlying pathways have not been well understood.
吕守芹 +9 more
core +1 more source
Interaction Networks Explain Holoenzyme Allostery in Protein Kinase A
Protein kinase A (PKA) signaling exemplifies phosphorylation-based signaling as we understand it today. Its catalytic-subunit structure and dynamics continue to advance our understanding of kinase mechanics as the first protein kinase catalytic domain to
Colin L. Welsh +2 more
core +1 more source
Citation: 'allostery' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.A00241 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
openaire +2 more sources
New experimental findings continue to challenge our understanding of protein allostery. Recent deep mutational scanning study showed that allosteric hotspots in the tetracycline repressor (TetR) and its homologous transcriptional factors are broadly ...
Zhuang Liu +3 more
doaj +1 more source
Complex networks of interacting residues and microdomains in the structures of biomolecular systems underlie the reliable propagation of information from an input signal, such as the concentration of a ligand, to sites that generate the appropriate ...
Michael V LeVine, Harel Weinstein
doaj +1 more source
Understanding how enzymes work: the journey to ensemble–function studies
For decades, structure–function has dominated biochemistry. Structures are highly valuable, yet more is needed to achieve a quantitative understanding of biomolecular function, because function emerges from an ensemble of states, rather than a static structure. We describe an ensemble–function framework applied to quantitatively dissect serine protease
Daniel Herschlag, Siyuan Du
wiley +1 more source
Allostery in Biomolecular Condensates
Allosteric proteins and membrane-less biomolecular condensates are physics-governed pivotal functional components. Allosteric regulation is an inherent physical property of dynamic proteins, and dynamic proteins are allosteric. Thus, in biomolecular condensates (like everywhere else in the cell), allostery is at play, and often missing in condensate ...
Ruth Nussinov, Clil Regev, Hyunbum Jang
openaire +3 more sources
PEG400 regulates Falcipain 2 activity through an allosteric mechanism
Falcipain‐2 can potentially be leveraged as a drug target due to its critical role as a haemoglobinase during the intra‐erythrocytic stage of Plasmodium falciparum. Here, we investigate the regulation of the proteolytic and haemoglobinase activity of falcipain‐2 in the presence of polyethylene glycol.
Bikram Nath +2 more
wiley +1 more source
Allosteric regulation of serine protease HtrA2 through novel non-canonical substrate binding pocket.
HtrA2, a trimeric proapoptotic serine protease is involved in several diseases including cancer and neurodegenerative disorders. Its unique ability to mediate apoptosis via multiple pathways makes it an important therapeutic target.
Pruthvi Raj Bejugam +6 more
doaj +1 more source
Differential impact of BTK active site inhibitors on the conformational state of full-length BTK
Bruton’s tyrosine kinase (BTK) is targeted in the treatment of B-cell disorders including leukemias and lymphomas. Currently approved BTK inhibitors, including Ibrutinib, a first-in-class covalent inhibitor of BTK, bind directly to the kinase active site.
Raji E Joseph +5 more
doaj +1 more source

