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1l6e

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[[Image:1l6e.gif|left|200px]]
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{{STRUCTURE_1l6e| PDB=1l6e | SCENE= }}
{{STRUCTURE_1l6e| PDB=1l6e | SCENE= }}
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'''Solution structure of the docking and dimerization domain of protein kinase A II-alpha (RIIalpha D/D). Alternatively called the N-terminal dimerization domain of the regulatory subunit of protein kinase A.'''
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===Solution structure of the docking and dimerization domain of protein kinase A II-alpha (RIIalpha D/D). Alternatively called the N-terminal dimerization domain of the regulatory subunit of protein kinase A.===
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==Overview==
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The structure of the N-terminal docking and dimerization domain of the type IIalpha regulatory subunit (RIIalpha D/D) of protein kinase A (PKA) forms a noncovalent stand-alone X-type four-helix bundle structural motif, consisting of two helix-loop-helix monomers. RIIalpha D/D possesses a strong hydrophobic core and two distinct, exposed faces. A hydrophobic face with a groove is the site of protein-protein interactions necessary for subcellular localization. A highly charged face, opposite to the former, may be involved in regulation of protein-protein interactions as a result of changes in phosphorylation state of the regulatory subunit. Although recent studies have addressed the hydrophobic character of packing of RIIalpha D/D and revealed the function of the hydrophobic face as the binding site to A-kinase anchoring proteins (AKAPs), little attention has been paid to the charges involved in structure and function. To examine the electrostatic character of the structure of RIIalpha D/D we have predicted mean apparent pKa values, based on Poisson-Boltzmann electrostatic calculations, using an ensemble of calculated dimer structures. We propose that the helix promoting sequence Glu34-X-X-X-Arg38 stabilizes the second helix of each monomer, through the formation of a (i, i +4) side chain salt bridge. We show that a weak inter-helical hydrogen bond between Tyr35-Glu19 of each monomer contributes to tertiary packing and may be responsible for discriminating from alternative quaternary packing of the two monomers. We also show that an inter-monomer hydrogen bond between Asp30-Arg40 contributes to quaternary packing. We propose that the charged face comprising of Asp27-Asp30-Glu34-Arg38-Arg40-Glu41-Arg43-Arg44 may be necessary to provide flexibility or stability in the region between the C-terminus and the interdomain/autoinhibitory sequence of RIIalpha, depending on the activation state of PKA. We also discuss the structural requirements necessary for the formation of a stacked (rather than intertwined) dimer, which has consequences for the orientation of the functionally important and distinct faces.
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{{ABSTRACT_PUBMED_11985580}}
==About this Structure==
==About this Structure==
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1L6E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6E OCA].
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1L6E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6E OCA].
==Reference==
==Reference==
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[[Category: Helix-loop-helix]]
[[Category: Helix-loop-helix]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:35:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:48:05 2008''

Revision as of 08:48, 2 July 2008

Image:1l6e.png

Template:STRUCTURE 1l6e

Solution structure of the docking and dimerization domain of protein kinase A II-alpha (RIIalpha D/D). Alternatively called the N-terminal dimerization domain of the regulatory subunit of protein kinase A.

Template:ABSTRACT PUBMED 11985580

About this Structure

1L6E is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

Electrostatic properties of the structure of the docking and dimerization domain of protein kinase A IIalpha., Morikis D, Roy M, Newlon MG, Scott JD, Jennings PA, Eur J Biochem. 2002 Apr;269(8):2040-51. PMID:11985580

Page seeded by OCA on Wed Jul 2 11:48:05 2008

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