Sandbox Reserved 822: Difference between revisions
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== '''Structure''' == | == '''Structure''' == | ||
The structure 1W1H has in total 4 chains. These are represented by 1 sequence-unique entity. | The structure 1W1H has in total 4 chains. These are represented by 1 sequence-unique entity. | ||
The PH domain of PDK1 reveals a structural variation of a standard PH domain fold with an additional 'bud' at the N-terminus. | The PH domain of PDK1 reveals a structural variation of a standard PH domain fold with an additional 'bud' at the N-terminus. | ||
The standard PH domain fold consists of mainly three different sections: | The standard PH domain fold consists of mainly three different sections: | ||
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*On the other side of the barrel three variable loops (VL 1-3) form a bowl-like structure which is lined by positively charged residues, consituting the phosphoinositide-binding site. | *On the other side of the barrel three variable loops (VL 1-3) form a bowl-like structure which is lined by positively charged residues, consituting the phosphoinositide-binding site. | ||
The PH domain of PDK1 possesses an additional extension N-terminal to the standard PH domain fold. This | The PH domain of PDK1 possesses an additional extension ('bud') N-terminal to the standard PH domain fold. This bud forms two additional β strands and one α helix and is an integral part of the overall fold. The two β strands β1' and β2'extend the β1 - β4 sheet in an antiparallel fashion through the formation of β sheet hydrogen bonds between β2'and β1. The α helix packs against this newly formed six stranded β sheet forming an additional <scene name='56/568020/Hydrophobic_core/1'>hydrophobic core</scene> outside of the standard PH domain fold. The bud binds to the β1 - β4 sheet by several additional hydrophobic contacts and buries more than 30% of the surface of the standard PH domain fold. | ||
