2j32
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THE ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND ACTIVITY OF(PRO)CASPASE-3
OverviewOverview
During maturation, procaspase-3 is cleaved at D175, which resides in a, linker that connects the large and small subunits. The intersubunit linker, also connects two active site loops that rearrange following cleavage and, in part, form the so-called loop bundle. As a result of chain cleavage, new hydrogen bonds and van der Waals contacts form among three active site, loops. The new interactions are predicted to stabilize the active site., One unresolved issue is the extent to which the loop bundle residues also, stabilize the procaspase active site. We examined the effects of replacing, four loop bundle residues (E167, D169, E173, and Y203) on the biochemical, and structural properties of the (pro)caspase. We show that replacing the, residues affects the activity of the procaspase as ... [(full description)]
About this StructureAbout this Structure
2J32 is a [Single protein] structure of sequence from [Homo sapiens] with ACE as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3., Feeney B, Pop C, Swartz P, Mattos C, Clark AC, Biochemistry. 2006 Nov 7;45(44):13249-63. PMID:17073446
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