Sandbox Reserved 822: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 18: Line 18:
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.


[[Image:Topology_Diagram_of_PH_domain_of_PDK1.JPG|left|320px|thumb|Fig.1 Topology diagram of the PH domain of PDK1. The colors of the different sections correspond to the coloring of the Jmol structure applet. <ref> PMID: 524332 </ref>]]  
[[Image:Topology_Diagram_of_PH_domain_of_PDK1.JPG|left|320px|thumb|Fig.1 Topology diagram of the PH domain of PDK1. The colors of the different sections correspond to the coloring of the Jmol structure applet. <ref name="Structural"> PMID: 524332 </ref>]]  


The standard PH domain fold consists of mainly three different sections:
The standard PH domain fold consists of mainly three different sections:
Line 25: Line 25:
*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 (<scene name='56/568020/Bud/1'>'bud'</scene>) N-terminal to the standard PH domain fold. This bud forms two additional &beta; strands and one &alpha; helix and is an integral part of the overall fold. The two &beta; strands &beta;1' and &beta;2'extend the &beta;1 - &beta;4 sheet in an antiparallel fashion through the formation of &beta; sheet hydrogen bonds between &beta;2'and &beta;1. The &alpha; helix packs against this newly formed six stranded &beta; 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 &beta;1 - &beta;4 sheet by several additional hydrophobic contacts and buries more than 30% of the surface of the standard PH domain fold. <ref> PMID: 524332 </ref>
The PH domain of PDK1 possesses an additional extension (<scene name='56/568020/Bud/1'>'bud'</scene>) N-terminal to the standard PH domain fold. This bud forms two additional &beta; strands and one &alpha; helix and is an integral part of the overall fold. The two &beta; strands &beta;1' and &beta;2'extend the &beta;1 - &beta;4 sheet in an antiparallel fashion through the formation of &beta; sheet hydrogen bonds between &beta;2'and &beta;1. The &alpha; helix packs against this newly formed six stranded &beta; 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 &beta;1 - &beta;4 sheet by several additional hydrophobic contacts and buries more than 30% of the surface of the standard PH domain fold. <ref name="Structural" />