New public database of AI-predicted protein structures could transform biology

2021 ◽  
Keyword(s):  
Protein Structures ◽  
Public Database ◽  
New Public

scholarly journals VgeneRepertoire.org identifies and stores variable genes of immunoglobulins and T-cell receptors from the genomes of jawed vertebrates

2014 ◽  
Author(s):  
David N Olivieri ◽  
Francisco Gambón-Deza
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
T Cell Receptors ◽  
Chromosome Region ◽  
Cell Receptor ◽  
Amino Acid Sequences ◽  
Public Database ◽  
Phylogenetic Studies ◽  
New Public ◽  
Web Repository

The VgeneRepertoire.org platform (http://vgenerepertoire.org) is a new public database repository for variable (V) gene sequences that encode immunoglobulin and T-cell receptor molecules. It identifies the nucleic and amino acid sequences of more than 20,000 genes, providing their exon location in either the contig, scaffold, or chromosome region, as well as locus information for more than 100 jawed vertebrate taxa whose genomes have been sequenced. This web repository provides support to immunologists interested in these molecules and aids in comparative phylogenetic studies.

scholarly journals HIV Proviral Sequence Database: A New Public Database for Near Full-Length HIV Proviral Sequences and Their Meta-Analyses

2020 ◽  
Vol 36 (1) ◽  
pp. 1-3 ◽  
Author(s):  
Wei Shao ◽  
Jigui Shan ◽  
Wei-Shau Hu ◽  
Elias Konstantine Halvas ◽  
John W. Mellors ◽  
...  
Keyword(s):  
Full Length ◽  
Sequence Database ◽  
Public Database ◽  
Proviral Sequence ◽  
New Public ◽  
Meta Analyses

New public database of expressed human genome

1998 ◽  
Vol 14 (6) ◽  
pp. 247
Author(s):  
J Sieja Hagerman
Keyword(s):  
Human Genome ◽  
Public Database ◽  
New Public

scholarly journals The Economic Impacts of COVID-19: Evidence from a New Public Database Built Using Private Sector Data

2020 ◽  
Author(s):  
Raj Chetty ◽  
John Friedman ◽  
Nathaniel Hendren ◽  
Michael Stepner ◽  
The Opportunity Insights Team
Keyword(s):  
Private Sector ◽  
Economic Impacts ◽  
Public Database ◽  
New Public ◽  
Sector Data

scholarly journals Simultaneous arteriole and venule segmentation with domain-specific loss function on a new public database

2018 ◽  
Vol 9 (7) ◽  
pp. 3153 ◽  
Author(s):  
Xiayu Xu ◽  
Rendong Wang ◽  
Peilin Lv ◽  
Bin Gao ◽  
Chan Li ◽  
...  
Keyword(s):  
Loss Function ◽  
Public Database ◽  
Specific Loss ◽  
Domain Specific ◽  
New Public

Insights into the biochemical and functional characterization of sortase E transpeptidase of Corynebacterium glutamicum

2019 ◽  
Vol 476 (24) ◽  
pp. 3835-3847 ◽  
Author(s):  
Aliyath Susmitha ◽  
Kesavan Madhavan Nampoothiri ◽  
Harsha Bajaj
Keyword(s):  
Protein Engineering ◽  
Cell Attachment ◽  
Functional Characterization ◽  
Protein Structures ◽  
Structural Similarity ◽  
Surface Proteins ◽  
Sortase A ◽  
Peptide Cleavage ◽  
New Findings

Most Gram-positive bacteria contain a membrane-bound transpeptidase known as sortase which covalently incorporates the surface proteins on to the cell wall. The sortase-displayed protein structures are involved in cell attachment, nutrient uptake and aerial hyphae formation. Among the six classes of sortase (A–F), sortase A of S. aureus is the well-characterized housekeeping enzyme considered as an ideal drug target and a valuable biochemical reagent for protein engineering. Similar to SrtA, class E sortase in GC rich bacteria plays a housekeeping role which is not studied extensively. However, C. glutamicum ATCC 13032, an industrially important organism known for amino acid production, carries a single putative sortase (NCgl2838) gene but neither in vitro peptide cleavage activity nor biochemical characterizations have been investigated. Here, we identified that the gene is having a sortase activity and analyzed its structural similarity with Cd-SrtF. The purified enzyme showed a greater affinity toward LAXTG substrate with a calculated KM of 12 ± 1 µM, one of the highest affinities reported for this class of enzyme. Moreover, site-directed mutation studies were carried to ascertain the structure functional relationship of Cg-SrtE and all these are new findings which will enable us to perceive exciting protein engineering applications with this class of enzyme from a non-pathogenic microbe.

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