Sandbox Reserved 717: Difference between revisions
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The receptor-binding domain can be compared to a flower bud. This flower bud has got 12 petals which are organised in a 3-fold symmetry. At the bottom there are the residues 406-432 they form the <scene name='Sandbox_Reserved_717/Mynewscene/4'>first petal </scene> , just above there are the residues 489-504 which form the <scene name='Sandbox_Reserved_717/Mynewscene/5'>second petal</scene> . The <scene name='Sandbox_Reserved_717/Mynewscene/6'>third petal </scene> is formed by the residues 450-470 and at the top there are the residues 470-480 and form the <scene name='Sandbox_Reserved_717/Mynewscene/7'>fourth petal</scene> . The complete and active receptor-binding domain is built by the trimeric protein. This trimeric proteine structure is stabilised by many inter-domain hydrogen bounds. These hydrogen bounds can have the profiles: main-chain-main-chain, main-chain-side-chain and side-chain-side-chain. | The receptor-binding domain can be compared to a flower bud. This flower bud has got 12 petals which are organised in a 3-fold symmetry. At the bottom there are the residues 406-432 they form the <scene name='Sandbox_Reserved_717/Mynewscene/4'>first petal </scene> , just above there are the residues 489-504 which form the <scene name='Sandbox_Reserved_717/Mynewscene/5'>second petal</scene> . The <scene name='Sandbox_Reserved_717/Mynewscene/6'>third petal </scene> is formed by the residues 450-470 and at the top there are the residues 470-480 and form the <scene name='Sandbox_Reserved_717/Mynewscene/7'>fourth petal</scene> . The complete and active receptor-binding domain is built by the trimeric protein. This trimeric proteine structure is stabilised by many inter-domain hydrogen bounds. These hydrogen bounds can have the profiles: main-chain-main-chain, main-chain-side-chain and side-chain-side-chain. | ||
==='''The LPS-Bindind Site <ref> doi:10.1038/nsb970</ref>'''=== | ==='''The LPS-Bindind Site <ref name=r2> doi:10.1038/nsb970</ref>'''=== | ||
The exact position of the lipo-polysaccharide(LPS)-binding site is not known. Proteolysis experiments showed, that it contains to the domain with the residues <scene name='Sandbox_Reserved_717/Mythirdscene/8'>397-517</scene>. Compared with the homologous bacteriophage T4-like strain AR1 sequence, which also binds to the same LPS core molecule like gp12, there can be some possible binding residues be assumed. | The exact position of the lipo-polysaccharide(LPS)-binding site is not known. Proteolysis experiments showed, that it contains to the domain with the residues <scene name='Sandbox_Reserved_717/Mythirdscene/8'>397-517</scene>. Compared with the homologous bacteriophage T4-like strain AR1 sequence, which also binds to the same LPS core molecule like gp12, there can be some possible binding residues be assumed. | ||
