TY - JOUR
T1 - MERITS
T2 - a web-based integrated Mycobacterial PE/PPE protein database
AU - He, Zhijie
AU - Wang, Cong
AU - Guo, Xudong
AU - Sun, Heyun
AU - Bi, Yue
AU - Pitt, Miranda E.
AU - Li, Chen
AU - Song, Jiangning
AU - Coin, Lachlan J.M.
AU - Li, Fuyi
N1 - Publisher Copyright:
© 2024 The Author(s). Published by Oxford University Press.
PY - 2024
Y1 - 2024
N2 - Motivation: PE/PPE proteins, highly abundant in the Mycobacterium genome, play a vital role in virulence and immune modulation. Understanding their functions is key to comprehending the internal mechanisms of Mycobacterium. However, a lack of dedicated resources has limited research into PE/PPE proteins. Results: Addressing this gap, we introduce MycobactERIal PE/PPE proTeinS (MERITS), a comprehensive 3D structure database specifically designed for PE/PPE proteins. MERITS hosts 22 353 non-redundant PE/PPE proteins, encompassing details like physicochemical properties, subcellular localization, post-translational modification sites, protein functions, and measures of antigenicity, toxicity, and allergenicity. MERITS also includes data on their secondary and tertiary structure, along with other relevant biological information. MERITS is designed to be user-friendly, offering interactive search and data browsing features to aid researchers in exploring the potential functions of PE/PPE proteins. MERITS is expected to become a crucial resource in the field, aiding in developing new diagnostics and vaccines by elucidating the sequence-structure-functional relationships of PE/PPE proteins.
AB - Motivation: PE/PPE proteins, highly abundant in the Mycobacterium genome, play a vital role in virulence and immune modulation. Understanding their functions is key to comprehending the internal mechanisms of Mycobacterium. However, a lack of dedicated resources has limited research into PE/PPE proteins. Results: Addressing this gap, we introduce MycobactERIal PE/PPE proTeinS (MERITS), a comprehensive 3D structure database specifically designed for PE/PPE proteins. MERITS hosts 22 353 non-redundant PE/PPE proteins, encompassing details like physicochemical properties, subcellular localization, post-translational modification sites, protein functions, and measures of antigenicity, toxicity, and allergenicity. MERITS also includes data on their secondary and tertiary structure, along with other relevant biological information. MERITS is designed to be user-friendly, offering interactive search and data browsing features to aid researchers in exploring the potential functions of PE/PPE proteins. MERITS is expected to become a crucial resource in the field, aiding in developing new diagnostics and vaccines by elucidating the sequence-structure-functional relationships of PE/PPE proteins.
UR - http://www.scopus.com/inward/record.url?scp=85189025229&partnerID=8YFLogxK
U2 - 10.1093/bioadv/vbae035
DO - 10.1093/bioadv/vbae035
M3 - Article
C2 - 38549946
AN - SCOPUS:85189025229
SN - 2635-0041
VL - 4
JO - Bioinformatics Advances
JF - Bioinformatics Advances
IS - 1
M1 - vbae035
ER -
