Amino and carboxyl termini are unique positions in a polypeptide. They tend to be exposed in folded three dimensional structures. Diversity and functional significance of C-terminal sequences have been appreciated from studies of PDZ and PEX domains. Signaling 14-3-3 protein signaling by recognizing phosphorylated peptides plays a critical role in a variety of biological processes, including oncogenesis. The preferential binding of 14-3-3 to phosphorylated C-terminal sequences, mode III, provides a means of regulated binding and considerably expands the substrate repertoire of 14-3-3 interaction partners.
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http://dx.doi.org/10.1016/j.febslet.2006.02.014 | DOI Listing |
Adv Sci (Weinh)
January 2025
Institute for Chemical Research (IIQ), Scientific Research Center "Isla de la Cartuja" (cicCartuja), University of Seville-CSIC, Avda. Americo Vespucio 49, Seville, 41092, Spain.
Gene duplication has allowed protein evolution toward novel functions and mechanisms. The differences between paralogous genes frequently rely on the sequence of disordered regions. For instance, in mammals, the chaperones ANP32A and ANP32B share a common evolutionary line and have some exchangeable functions based on their similar N-terminal domains.
View Article and Find Full Text PDFJ Med Chem
January 2025
Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
Measles is a highly infectious disease and remains a major cause of childhood mortality worldwide. In some cases, the measles virus (MV) induces subacute sclerosing panencephalitis within several years of the acute infection. The infection of the target cells by MV is mediated by the F protein, in which two heptad repeat regions, HR1 and HR2, form a six-helix bundle before membrane fusion.
View Article and Find Full Text PDFRNA
January 2025
Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Uniwersytetu Poznanskiego 6, 61-614 Poznan, Poland
Neisseria meningitidis minimal ProQ is a global RNA binding protein belonging to the family of FinO-domain proteins. The N. meningitidis ProQ consists only of the FinO domain accompanied by short N- and C-terminal extensions.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, United States.
The mammalian high mobility group protein AT-hook 2 (HMGA2) is a small DNA-binding protein that specifically targets AT-rich DNA sequences. Structurally, HMGA2 is an intrinsically disordered protein (IDP), comprising three positively charged 'AT-hooks' and a negatively charged C-terminus. HMGA2 can form homodimers through electrostatic interactions between its 'AT-hooks' and C-terminus.
View Article and Find Full Text PDFMol Biol Rep
January 2025
Department of Gastroenterology, Beijing Friendship Hospital, Capital Medical University, No. 95, Yong An Road, Xi Cheng District, Beijing, 100050, China.
Canopy family proteins are highly sequence-conserved proteins with an N-terminal hydrophobic signal sequence, a unique pattern of six cysteine residues characteristic of the saposin-like proteins, and a C-terminal putative endoplasmic reticulum retention signal sequence. At present, the known canopy family proteins are canopy fibroblast growth factor signaling regulator 1 (CNPY1), CNPY2, CNPY3, and CNPY4. Despite similar structures, canopy family proteins regulate complex signal networks to participate in various biological processes.
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