P53R2: Difference between revisions
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The N-terminal residues of the monomer A can stabilize the B helix of the monomer B due to different interactions. R41 of the monomer A forms a salt bridge with E119 of monomer A. This interaction permits the formation of a H-bond between R40 of monomer A with G101of monomer B. Furthermore K37 in monomer A forms a salt bridge with E105 of monomer B and this stabilize its B helix. All the interactions allow D100 of monomer B to be well oriented to bind Fe1 (see Figure below, Smith P. et al., <ref>PMID:19728742</ref>). | The N-terminal residues of the monomer A can stabilize the B helix of the monomer B due to different interactions. R41 of the monomer A forms a salt bridge with E119 of monomer A. This interaction permits the formation of a H-bond between R40 of monomer A with G101of monomer B. Furthermore K37 in monomer A forms a salt bridge with E105 of monomer B and this stabilize its B helix. All the interactions allow D100 of monomer B to be well oriented to bind Fe1 (see Figure below, Smith P. et al., <ref>PMID:19728742</ref>). | ||
[[Image:Figure 1.jpg | thumb | center]] | [[Image:Figure 1.jpg | thumb | Shown are the interactions between the N-terminal loop of monomer A and the continuous helix B of monomer B with the iron binding sites Fe1 and Fe2. | center]] | ||
On the contrary R40 of monomer B is bound to E119 of the same monomer and so it can not bind to G101 of the monomer A and the consequence is that F42 disturb the B helix of monomer A. D100 can not interact with Fe1. This explain why the monomer A has only one iron-binding site whereas the monomer B has two (see Figure below, Smith P. et al. <ref>PMID:19728742</ref>). | On the contrary R40 of monomer B is bound to E119 of the same monomer and so it can not bind to G101 of the monomer A and the consequence is that F42 disturb the B helix of monomer A. D100 can not interact with Fe1. This explain why the monomer A has only one iron-binding site whereas the monomer B has two (see Figure below, Smith P. et al. <ref>PMID:19728742</ref>). | ||
[[Image:Figure 2.jpg | thumb | center]] | [[Image:Figure 2.jpg | thumb | Shown are the interactions between the N-terminal loop of monomer B and the discontinuous helix B of monomer A with the iron binding site Fe2. | center]] | ||
Compare to the M2 subunit, these iron-binding sites are less efficient. This is due to the different conformations that the p53R2 subunit can adopt (stabilization or not of the two helix B and D). | Compare to the M2 subunit, these iron-binding sites are less efficient. This is due to the different conformations that the p53R2 subunit can adopt (stabilization or not of the two helix B and D). | ||