Literature summary for 3.4.21.47 extracted from

Forneris, F.; Ricklin, D.; Wu, J.; Tzekou, A.; Wallace, R.; Lambris, J.; Gros, P.
Structures of C3b in complex with factors B and D give insight into complement convertase formation (2010), Science, 330, 1816-1820.

Search for more literature for 3.4.21.47

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the pro-convertase C3bB at 4 A resolution and its complex with factor D at 3.5 A resolution. Factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor Ds self-inhibitory loop. This concerted proteolytic mechanism, which is cofactordependent and substrate-induced, restricts complement amplification to C3b-tagged target cells	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of the pro-convertase C3bB at 4 A resolution and its complex with factor D at 3.5 A resolution. Factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor Ds self-inhibitory loop. This concerted proteolytic mechanism, which is cofactordependent and substrate-induced, restricts complement amplification to C3b-tagged target cells

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P01024	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to yield C5a and C5b	factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D's self-inhibitory loop. This concerted proteolytic mechanism, which is cofactor-dependent and substrate-induced, restricts complement amplification to C3b-tagged target cells	Homo sapiens	a

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)