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 LPS-Bindind Site <ref> doi:10.1038/nsb970</ref>==

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==3.)Zinc==

The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids <scene name='Sandbox_Reserved_717/Mynewscene/3'>His445 and His447 </scene> of each monomer. The distances of the zinc ion to the NE2 of (<scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene>) are 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.

The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids <scene name='Sandbox_Reserved_717/Mynewscene/3'>His445 and His447 </scene> of each monomer. The distances of the zinc ion to the NE2 of <scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene> are 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.

The role of the zinc ion is probably absolute of structural nature. It increases the stability of the C-terminus of gp12 against proteases, but it also raises the stability of the C-terminus in general.

Sandbox Reserved 717: Difference between revisions

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@@ Line 62: / Line 62: @@
 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>==
@@ Line 89: / Line 86: @@
 ==3.)Zinc==
-The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids <scene name='Sandbox_Reserved_717/Mynewscene/3'>His445 and His447  </scene>  of each monomer. The distances of the zinc ion to the NE2 of (<scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene>)  are 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.
+The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids <scene name='Sandbox_Reserved_717/Mynewscene/3'>His445 and His447  </scene>  of each monomer. The distances of the zinc ion to the NE2 of <scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene> are 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.
 The role of the zinc ion is probably absolute of structural nature. It increases the stability of the C-terminus of gp12 against proteases, but it also raises the stability of the C-terminus in general.