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Figure 1 | BMC Biochemistry

Figure 1

From: Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B

Figure 1

Domain architecture and sequences of human and mouse BNIP-2. A. Known or putative functional motifs indicated are: the Rho-binding domain (RBD), Cdc42/Rac1-Interactive Binding (CRIB)-like motif, BCH signature motif, BCH/BCH interaction motif, caspase and granzyme cleavage sites and kinesin-targeting motifs. Annotation of the RBD is based on close similarity to known RBDs in BNIP-2 homologs and Cdc42GAP. B. ClustalW multiple sequence alignment of human and mouse BNIP-2 splice variants, i.e., the database annotated hBNIP2 sequence [Swiss-Prot: Q12982] as well as short mBNIP-2 [Trembl: Q91VL0] and long mBNIP-2 [Swiss-Prot: O54940]. The black box highlights the P4-P9′ motif with the P4-P1 IEAD GrB cleavage motif and BNIP-2 domains indicated as in A.

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