Sandbox Reserved 818: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 30: Line 30:
. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins [73]. <br />
. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins [73]. <br />


The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus <scene name='56/568016/Ptx_asn105/1'>Asn105</scene> in ''S2'' and '''Lys103''' in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes  
The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus <scene name='56/568016/Ptx_asn105/1'>Asn105</scene> in ''S2'' and <scene name='56/568016/Ptx_lys105/1'>Lys105</scene> in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes  
<ref name="Locht93">
<ref name="Locht93">
Lobet, Y., Feron, C., Dequesne, G., Simoen, E., Hauser, P., & Locht, C. (1993). Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin. The Journal of experimental medicine, 177(1), 79-87.
Lobet, Y., Feron, C., Dequesne, G., Simoen, E., Hauser, P., & Locht, C. (1993). Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin. The Journal of experimental medicine, 177(1), 79-87.