Sandbox Reserved 702: Difference between revisions
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This domain exposes a richly negative-charged surface which easily interacts with the positively charged residues of the protective antigen. Edema factor's protective antigen-binding domain can be divided into two subdomains. | This domain exposes a richly negative-charged surface which easily interacts with the positively charged residues of the protective antigen. Edema factor's protective antigen-binding domain can be divided into two subdomains. | ||
<scene name='Sandbox_Reserved_702/Secondary_structure/1'>Secondary structure of 1lvc.</scene> {{Template:ColorKey_Helix}} | <scene name='Sandbox_Reserved_702/Secondary_structure/1'>Secondary structure of 1lvc.</scene> ({{Template:ColorKey_Helix}}and | ||
{{Template:ColorKey_Strand}} | {{Template:ColorKey_Strand}}) | ||
The N-terminal domain is composed of three layers, α/β sandwich domain (four β-sheets β1 to β4, in sandwich between four α-helices α1 to α4). The C-terminal domain is composed of five helices. | The N-terminal domain is composed of three layers, α/β sandwich domain (four β-sheets β1 to β4, in sandwich between four α-helices α1 to α4). The C-terminal domain is composed of five helices. | ||
The protective antigen-binding domain contains five joining loops L1 to L5, and L5 has the key exposed residues that bind to the protective antigen. Residues in α6, α7 and in the joining loop between α7 and α8 at the C-terminal domain are also implied in the interaction. <ref> PMID: 15719022</ref> | The protective antigen-binding domain contains five joining loops L1 to L5, and L5 has the key exposed residues that bind to the protective antigen. Residues in α6, α7 and in the joining loop between α7 and α8 at the C-terminal domain are also implied in the interaction. <ref> PMID: 15719022</ref> | ||
