Literature summary for 1.2.1.12 extracted from

Nagata, H.; Iwasaki, M.; Maeda, K.; Kuboniwa, M.; Hashino, E.; Toe, M.; Minamino, N.; Kuwahara, H.; Shizukuishi, S.
Identification of binding domain of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase for Porphyromonas gingivalis major fimbriae (2009), Infect. Immun., 77, 5130-5138.

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Organism

Organism	UniProt	Comment	Textmining
Streptococcus oralis	-	-	-

Subunits

Subunits	Comment	Organism
More	interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA	Streptococcus oralis

General Information

General Information	Comment	Organism
physiological function	interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA	Streptococcus oralis

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Release 2023.1 (January 2023)