The latest version of the CATH-Gene3D protein structure classification database has recently been released (version 4.1, http://www.cathdb.info). The resource comprises over 300 000 domain structures and over 53 million protein domains classified into 2737 homologous superfamilies, doubling the number of predicted protein domains in the previous version. The daily-updated CATH-B, which contains our very latest domain assignment data, provides putative classifications for over 100 000 additional protein domains. This article describes developments to the CATH-Gene3D resource over the last two years since the publication in 2015, including: significant increases to our structural and sequence coverage; expansion of the functional families in CATH; building a support vector machine (SVM) to automatically assign domains to superfamilies; improved search facilities to return alignments of query sequences against multiple sequence alignments; the redesign of the web pages and download site.
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http://dx.doi.org/10.1093/nar/gkw1098 | DOI Listing |
Sci Rep
December 2024
Department of Life Sciences, Pohang University of Science and Technology, Pohang, 37673, Kyungbook, Republic of Korea.
Alanine racemase (Alr) catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization between L- and D-alanine in bacteria. Owing to the potential interest in targeting Alr for antibacterial drug development, several studies have determined the structures of Alr from different species, proposing models for the reaction mechanism. Insights into its reaction dynamics may be conducive to a better understanding of the Alr reaction mechanism.
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December 2024
Department of Anatomy, Faculty of Science, Mahidol University, 272 Rama VI Road, Ratchathewi, Bangkok, 10400, Thailand.
SARS-CoV-2, the cause of COVID-19, primarily targets lung tissue, leading to pneumonia and lung injury. The spike protein of this virus binds to the common receptor on susceptible tissues and cells called the angiotensin-converting enzyme-2 (ACE2) of the angiotensin (ANG) system. In this study, we produced chimeric Macrobrachium rosenbergii nodavirus virus-like particles, presenting a short peptide ligand (ACE2tp), based on angiotensin-II (ANG II), on their outer surfaces to allow them to specifically bind to ACE2-overexpressing cells called ACE2tp-MrNV-VLPs.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, TEDA, Tianjin 300457, PR China; Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin 300457, PR China. Electronic address:
The robustness and catalytic activity of superoxide dismutase (SOD) are still the main factors limiting their application in industrial fields. This study aims to further improve the properties of a natural thermophilic iron/manganese dual-domain SOD (Fe/Mn-SODA fused with N-terminal polypeptide) from Geobacillus thermodenitrificans NG80-2 (GtSOD) by modifying its each domain using in-depth in silico prediction analysis as well as protein engineering. First, computational analysis of the N-terminal domain and GtSODA domain was respectively performed by using homologous sequence alignment and virtual mutagenesis.
View Article and Find Full Text PDFColloids Surf B Biointerfaces
December 2024
Laboratory of Applied Toxicology, Center of Toxins, Immune-Response and Cell Signaling - CeT-ICS/CEPID, Butantan Institute São Paulo, São Paulo, SP CEP 05503-900, Brazil; Postgraduate Program Interunits in Biotechnology, USP/IPT/IBU, São Paulo, SP, Brazil. Electronic address:
Background: Irresponsible and wholesale use of antimicrobial agents is the principal cause of the emergence of strains of resistant microorganisms to traditional drugs. Oligoventin is a neutral peptide isolated from spider eggs of Phoneutria nigriventer, with antimicrobial activity against Gram-positive, Gram-negative, and yeast organisms. However, the molecular target and pathways of antimicrobial activity are still unknown.
View Article and Find Full Text PDFProtein Sci
January 2025
Department of Neuroscience, Biomedicine and Movement Sciences, Section of Biochemistry, University of Verona, Verona, Italy.
Human succinic semialdehyde dehydrogenase is a mitochondrial enzyme fundamental in the neurotransmitter γ-aminobutyric acid catabolism. It catalyzes the NAD-dependent oxidative degradation of its derivative, succinic semialdehyde, to succinic acid. Mutations in its gene lead to an inherited neurometabolic rare disease, succinic semialdehyde dehydrogenase deficiency, characterized by mental and developmental delay.
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