Literature summary for 3.4.21.104 extracted from

Nan, R.; Furze, C.M.; Wright, D.W.; Gor, J.; Wallis, R.; Perkins, S.J.
Flexibility in mannan-binding lectin-associated serine proteases-1 and -2 provides insight on lectin pathway activation (2017), Structure, 25, 364-375 .

Search for more literature for 3.4.21.104

Cloned(Commentary)

Cloned (Comment)	Organism
-	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of Ca2+-bound MASP dimers. Solution structures of the CUB1-EGF-CUB2 dimer indicate that the two CUB2 domains are tilted by 90 degreees compared with the crystal structures. Solution structures of the full-length MASP dimers in their zymogen and activated forms reveal similar structures that are much more bent than anticipated. MASP-2 and its activator MASP-1 are flexible at multiple sites and this flexibility may permit both intra- and inter-complex activation	Rattus norvegicus

Crystallization (Comment)

Organism

structures of Ca2+-bound MASP dimers. Solution structures of the CUB1-EGF-CUB2 dimer indicate that the two CUB2 domains are tilted by 90 degreees compared with the crystal structures. Solution structures of the full-length MASP dimers in their zymogen and activated forms reveal similar structures that are much more bent than anticipated. MASP-2 and its activator MASP-1 are flexible at multiple sites and this flexibility may permit both intra- and inter-complex activation

Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q9JJS8	-	-

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)