Sandbox Reserved 822

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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.
Connsidering the structure, several different sections can be found which explain altogether the function of the PH domain.
Connsidering the structure, several different sections can be found which explain altogether the function of the PH domain.
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One section is a <scene name='56/568020/Barrel-like/3'>barrel-like structure</scene> formed by residues 456-530.
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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, &beta; sheets, one consisting of four (&beta;1 - &beta;4) and one of three (&beta;5 -&beta;7) strands.

Revision as of 13:22, 4 January 2014

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.
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PDB ID 1w1h

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1w1h, resolution 1.45Å ()
Ligands: ,
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Related: 1h1w, 1oky, 1okz, 1uu3, 1uu7, 1uu8, 1uu9, 1uvr, 1w1d, 1w1g
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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.

PDK1 contains 556 amino acids and phosphorylates and activates at least 24 Proteins of the AGC (cAMP-dependent, cGMP-dependent, protein kinase C (PKC)) family of protein kinases. It therefore consists of a N-terminal Ser/Thr kinase catalytic domain (residues 71-359) and the C-terminal pleckstrin homology (PH) domain (residues 459-550).

PDK1 is activated by binding of its PH domain to specific target molecules like phosphoinositides or phosphoatityl inositides and can then interact with its target substrates.

Even though the targeting of PDK1 to specific locations of the cell is not fully understand in detail, it has been proven that the binding of its PH domain to target molecules plays a central role in this process.


Structure

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. Connsidering the structure, several different sections can be found which explain altogether the function of the PH domain. One section is a 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) strands.

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