收藏切换
Study of protein interaction based on the triplets combination pairs of the residue groups
收藏切换
PDF
Wei XIAO1, 2, Zeng-hui HE2, Shi-liang LI2, Hong-lin LI1, 2, *
Acta Pharmaceutica Sinica | 2017, 52(10) : 1578 - 1586
Less
收藏切换
Acta Pharmaceutica Sinica | 2017, 52(10): 1578-1586
ORIGINAL ARTICLES
Study of protein interaction based on the triplets combination pairs of the residue groups
Full
Wei XIAO1, 2, Zeng-hui HE2, Shi-liang LI2, Hong-lin LI1, 2, *
Affiliations
  • 1. School of Information Science and Engineering, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China
  • 2. Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China
Published: 2017-10-12 doi: 10.16438/j.0513-4870.2017-0419
Outline
收藏切换

The protein-protein interactions play an important role in life science. At present, many methods are developed with preferences of the amino acid residues, which do not offer the relative spatial information for the residue groups. However, the spatial information for the residue groups is important in the design of the protein-protein interactions. We proposed a new model, which is named 'tri-prism' model, by deep mining the existing protein-protein interaction patterns and refining the preference and the relative spatial information for the combination pairs of the residue groups. The model not only provided the preferences, but also offered the relative spatial information for the triplets combination pairs of the residue groups. The model was able to analyze the triplets combination pairs of the residue groups based on the preference factor, amino acid composition, and protein secondary structure. The model was applied to the interface of the PD-1/PD-L2 protein. According to the diversity characters of the composition and the spatial information between the combination pairs of the residue groups at the interface of the PD-1/PD-L2 protein and the predicted ones, we put forward the suggestions for the mutations of the residues, which offered a new view in the study of protein-protein interactions.

protein-protein interaction  /  'tri-prism' model  /  the triplets combination pairs of the residue group
Wei XIAO, Zeng-hui HE, Shi-liang LI, Hong-lin LI. Study of protein interaction based on the triplets combination pairs of the residue groups[J]. Acta Pharmaceutica Sinica, 2017 , 52 (10) : 1578 -1586 . DOI: 10.16438/j.0513-4870.2017-0419
Year 2017 volume 52 Issue 10
PDF
166
63
Cite this Article
BibTeX
Article Info
doi: 10.16438/j.0513-4870.2017-0419
  • Receive Date:2017-05-02
  • Online Date:2026-01-14
  • Published:2017-10-12
Article Data
Affiliations
History
  • Received:2017-05-02
  • Revised:2017-06-23
Funding
Affiliations
    1. School of Information Science and Engineering, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China
    2. Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China
References
Share
https://castjournals.cast.org.cn/joweb/yxxb/EN/10.16438/j.0513-4870.2017-0419
Share to
QR

Scan QR to access full text

Cite this article
BibTeX
Citations
表12种不同金属材料的力学参数

Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)

Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
关闭全屏
  • BibTeX
  • EndNote
  • RefWorks
  • TxT