Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.

Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.

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About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases, but the structural details of kinase inactivation have remained unclear. We present the first structure of a pseudokinase, VRK3, and that of its closest active relative, VRK2. Profound changes to the active si...

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Номзүйн дэлгэрэнгүй
Үндсэн зохиолчид:	Scheeff, E, Eswaran, J, Bunkoczi, G, Knapp, S, Manning, G
Формат:	Journal article
Хэл сонгох:	English
Хэвлэсэн:	2009

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