Sandbox Reserved 717: Difference between revisions
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Like the 33kDa fragment the 45kDa fragment can also be divided into two subunits. These two subunits are called head (residues <scene name='Sandbox_Reserved_717/Mythirdscene/5'>397-446 </scene> and residues <scene name='Sandbox_Reserved_717/Mythirdscene/6'>487-517</scene> ) and <scene name='Sandbox_Reserved_717/Mythirdscene/7'>bonnet</scene> (residues 447-487). On the border between the head and the bonnet subunit there is a metal-binding site. | Like the 33kDa fragment the 45kDa fragment can also be divided into two subunits. These two subunits are called head (residues <scene name='Sandbox_Reserved_717/Mythirdscene/5'>397-446 </scene> and residues <scene name='Sandbox_Reserved_717/Mythirdscene/6'>487-517</scene> ) and <scene name='Sandbox_Reserved_717/Mythirdscene/7'>bonnet</scene> (residues 447-487). On the border between the head and the bonnet subunit there is a metal-binding site. | ||
==='''Receptor-Binding Domain <ref> doi:10.1038/nsb970</ref>''' === | ==='''Receptor-Binding Domain <ref name=r2> doi:10.1038/nsb970</ref>''' === | ||
Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues <scene name='Sandbox_Reserved_717/Mythirdscene/8'>397-517</scene>. They are referred to be part of the receptor-binding domain. | Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues <scene name='Sandbox_Reserved_717/Mythirdscene/8'>397-517</scene>. They are referred to be part of the receptor-binding domain. | ||
The receptor-binding domain can be sub-divided into head and bonnet. On the border between these two subdomains there is a metal-binding site. This site binds presumably to zinc. <scene name='Sandbox_Reserved_717/Mynewscene/3'>Two His amino acids </scene> (<scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene>) from each monomere are octahedrally coordinated around the zinc. | The receptor-binding domain can be sub-divided into head and bonnet. On the border between these two subdomains there is a metal-binding site. This site binds presumably to zinc. <scene name='Sandbox_Reserved_717/Mynewscene/3'>Two His amino acids </scene> (<scene name='Sandbox_Reserved_717/Mynewscene/1'>His445</scene> and <scene name='Sandbox_Reserved_717/Mynewscene/2'>His447</scene>) from each monomere are octahedrally coordinated around the zinc. | ||
