G14secL04Tpc3: Difference between revisions

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on this loop. This important lysine forms an ionic salt bridge with the <scene name='G14secL04Tpc3/Lysine-253_and_glu50/2'>glutamic acid at residue 50</scene>
on this loop. This important lysine forms an ionic salt bridge with the <scene name='G14secL04Tpc3/Lysine-253_and_glu50/2'>glutamic acid at residue 50</scene>
on the heavy chain of the antibody Fab Fragment. Thus, formation of the complex consist of the C-terminus of the OspB protein coming into contact with the variable regions of the H6831 antibody Fab fragment and the lysine-253 wedging between the two <scene name='G14secL04Tpc3/Lysine-253_glu50_tyr_and_trp/2'>aromatic residues</scene>
on the heavy chain of the antibody Fab Fragment. Thus, formation of the complex consist of the C-terminus of the OspB protein coming into contact with the variable regions of the H6831 antibody Fab fragment and the lysine-253 wedging between the two <scene name='G14secL04Tpc3/Lysine-253_glu50_tyr_and_trp/2'>aromatic residues</scene>
(tryptophan-33 and tyrosine-101) and salt bridging with the glu-50 on the heavy chain of the antibody<ref name ="1rjl_pdb" />. Studies show that other bacterial strains having a cysteine, glycine, glutamic acid, or threonine in place of Lys-253 demonstrate resistance to the bactericidal effects of H6831 and also less binding affinity for the antibody Fab fragment (citation needed). This bolsters how important the Lys-253 is in the binding between the OspB protein and the antibody. After the complex is formed and the first four beta strands are cleaved off, a relic of this loss is a single <scene name='G14secL04Tpc3/Freely_floating_beta_strand/2'>freely floating beta strand</scene> on the N-terminus of the protein. This beta strand plays a role in the formation of dimers of OspB∙H6831 complex(citation). Although the second loop bearing the lysine is very important, the other loops certainly contribute to the bonding between OspB and the antibody fab fragment. For example, a <scene name='G14secL04Tpc3/Threonine_and_light_chain/1'>threonine</scene>
(tryptophan-33 and tyrosine-101) and salt bridging with the glu-50 on the heavy chain of the antibody<ref name ="1rjl_pdb" />. Studies show that other bacterial strains having a cysteine, glycine, glutamic acid, or threonine in place of Lys-253 demonstrate resistance to the bactericidal effects of H6831 and also less binding affinity for the antibody Fab fragment <ref>http://iai.asm.org/content/62/5/2037.short</ref>. This bolsters how important the Lys-253 is in the binding between the OspB protein and the antibody. After the complex is formed and the first four beta strands are cleaved off, a relic of this loss is a single <scene name='G14secL04Tpc3/Freely_floating_beta_strand/2'>freely floating beta strand</scene> on the N-terminus of the protein. This beta strand plays a role in the formation of dimers of OspB∙H6831 complex(citation). Although the second loop bearing the lysine is very important, the other loops certainly contribute to the bonding between OspB and the antibody fab fragment. For example, a <scene name='G14secL04Tpc3/Threonine_and_light_chain/1'>threonine</scene>
at residue 276 on another loop interacts with residues on the light chain of the antibody fragment.
at residue 276 on another loop interacts with residues on the light chain of the antibody fragment.


==References==
==References==
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