G04SecL04Tpc1
From Proteopedia
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The complex formed by the C-terminal end of Outer Surface Protein B and H6831 displays a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple,Binding with the Fab region of the H6831, light blue. | The complex formed by the C-terminal end of Outer Surface Protein B and H6831 displays a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple,Binding with the Fab region of the H6831, light blue. | ||
| - | There are three loop regions on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two and the Fab heavy chain. More minor hydrogen bonding interactions occur between loop one and the heavy chain as well as loop three and the light chains. The essential residue on loop two is the <scene name='G04SecL04Tpc1/Osp_b_fab_complex/2'>lysine at position 253 </scene> shown in green. This lysine forms an ion pair with a glutamic acid, red, of the Fab heavy chain. This bond is locked in by the presence of two aromatic residues that reside on the Fab, tryptophan and tyrosine shown in black. This antigen-antibody complex is further stabilized by the presence of a threonine, orange, on the 276 position. There are some instances in which the H6831 cannot bind to Osp-B. This is a case of a mutant form of the protein in which the essential lysine is replaced by another residue. | + | There are three loop regions on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two and the Fab heavy chain. More minor hydrogen bonding interactions occur between loop one and the heavy chain as well as loop three and the light chains. The essential residue on loop two is the <scene name='G04SecL04Tpc1/Osp_b_fab_complex/2'>lysine at position 253 </scene> shown in green. This lysine forms an ion pair with a glutamic acid, red, of the Fab heavy chain. This bond is locked in by the presence of two aromatic residues that reside on the Fab, tryptophan and tyrosine shown in black. This antigen-antibody complex is further stabilized by the presence of a threonine, orange, on the 276 position. There are some instances in which the H6831 cannot bind to Osp-B. This is a case of a mutant form of the protein in which the essential lysine is replaced by another residue. |
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| + | Upon binding, Osp-B experiences structural changes, the largest being the disappearance of the first four beta sheets. The loop opposite the Fab binding site along with the putative N-terminal region and a non-epitope loop also experience conformational changes all in which shift towards the missing beta sheets. | ||
Revision as of 03:07, 15 August 2012
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Osp-B H6831 complex
The complex formed by the C-terminal end of Outer Surface Protein B and H6831 displays a , purple,Binding with the Fab region of the H6831, light blue.
There are three loop regions on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two and the Fab heavy chain. More minor hydrogen bonding interactions occur between loop one and the heavy chain as well as loop three and the light chains. The essential residue on loop two is the shown in green. This lysine forms an ion pair with a glutamic acid, red, of the Fab heavy chain. This bond is locked in by the presence of two aromatic residues that reside on the Fab, tryptophan and tyrosine shown in black. This antigen-antibody complex is further stabilized by the presence of a threonine, orange, on the 276 position. There are some instances in which the H6831 cannot bind to Osp-B. This is a case of a mutant form of the protein in which the essential lysine is replaced by another residue.
Upon binding, Osp-B experiences structural changes, the largest being the disappearance of the first four beta sheets. The loop opposite the Fab binding site along with the putative N-terminal region and a non-epitope loop also experience conformational changes all in which shift towards the missing beta sheets.
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this is ospa binding to fab LA-2 ala 208
