Sandbox Reserved 822: Difference between revisions
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{{STRUCTURE_1w1h| PDB=1w1h | SCENE= }} | {{STRUCTURE_1w1h| PDB=1w1h | SCENE= }} | ||
== '''Description''' == | == '''Description''' == | ||
1w1h is a 4 chain structure of the human pleckstrin homology (PH) domain of the 3-phosphoinositide-dependent protein kinase 1 (PDK1), which plays a various role in PI3K signaling pathways. | 1w1h is a 4 chain structure of the human pleckstrin homology (PH) domain of the 3-phosphoinositide-dependent protein kinase 1 (PDK1), which plays a various role in PI3K signaling pathways. | ||
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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. | ||
One section is a <scene name='56/568020/Barrel-like/3'>barrel-like structure</scene> formed by residues 456-530 (only shown on chain D). This structure is formed by two, almost orthogonal, β sheets, one consisting of four (β1 - β4) and one of three (β5 - β7) stand. | The standard PH domain fold consists of mainly three different sections: | ||
One side of the barrel is blocked by a <scene name='56/568020/Alpha1/1'>C-terminal alpha helix</scene>. | *One section is a <scene name='56/568020/Barrel-like/3'>barrel-like structure</scene> formed by residues 456-530 (only shown on chain D). This structure is formed by two, almost orthogonal, β sheets, one consisting of four (β1 - β4) and one of three (β5 - β7) stand. | ||
On the other side of the barrel three variable loops (VL 1-3) form a bowl-like structure | *One side of the barrel is blocked by a <scene name='56/568020/Alpha1/1'>C-terminal alpha helix</scene>. | ||
*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 'bud' forms two additional β strands and one α helix. 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. | |||
