Cross-Species Analyses Identify the BNIP-2 and Cdc42GAP Homology (BCH) Domain as a Distinct Functional Subclass of the CRAL_TRIO/Sec14 Superfamily
Figure 4
Predicted three dimensional structures of BCH domains.
(a) A predicted three dimensional structure of the HsBNIP-2 BCH domain is displayed in this figure. The highly conserved proline residues are shown in yellow in a sphere representation. They are positioned in loops connecting the β-strands and α-helices. The patch of positively charged residues (called as Arg/Lys patch) is highlighted in blue color and the highly conserved residues H248, K271 are marked. (b) The side-chain of K271 comes in close contact with the backbone oxygen of R238 in the Arg/Lys patch (shown in zoomed box). This predicted interaction could provide added stability to the helical loop, which likely gates a lipid-binding cavity. (c) The side-chain of N189 from the Rho-binding region interacts with the side-chain of D143 of N-terminus α-helix (distance: 2.7 Å). This indicates that the N-terminus helix might be involved in Rho binding activity.