1cx4
From Proteopedia
(New page: 200px<br /><applet load="1cx4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cx4, resolution 2.45Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1cx4.jpg|left|200px]]<br /><applet load="1cx4" size=" | + | [[Image:1cx4.jpg|left|200px]]<br /><applet load="1cx4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cx4, resolution 2.45Å" /> | caption="1cx4, resolution 2.45Å" /> | ||
'''CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE'''<br /> | '''CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Cyclic AMP binding domains possess common structural features | + | BACKGROUND: Cyclic AMP binding domains possess common structural features yet are diversely coupled to different signaling modules. Each cAMP binding domain receives and transmits a cAMP signal; however, the signaling networks differ even within the same family of regulatory proteins as evidenced by the long-standing biochemical and physiological differences between type I and type II regulatory subunits of cAMP-dependent protein kinase. RESULTS: We report the first type II regulatory subunit crystal structure, which we determined to 2.45 A resolution and refined to an R factor of 0.176 with a free R factor of 0.198. This new structure of the type II beta regulatory subunit of cAMP-dependent protein kinase demonstrates that the relative orientations of the two tandem cAMP binding domains are very different in the type II beta as compared to the type I alpha regulatory subunit. Each structural unit for binding cAMP contains the highly conserved phosphate binding cassette that can be considered the "signature" motif of cAMP binding domains. This motif is coupled to nonconserved regions that link the cAMP signal to diverse structural and functional modules. CONCLUSIONS: Both the diversity and similarity of cAMP binding sites are demonstrated by this new type II regulatory subunit structure. The structure represents an intramolecular paradigm for the cooperative triad that links two cAMP binding sites through a domain interface to the catalytic subunit of cAMP-dependent protein kinase. The domain interface surface is created by the binding of only one cAMP molecule and is enabled by amino acid sequence variability within the peptide chain that tethers the two domains together. |
==About this Structure== | ==About this Structure== | ||
| - | 1CX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CMP:'>CMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Diller, T | + | [[Category: Diller, T C.]] |
| - | [[Category: Taylor, S | + | [[Category: Taylor, S S.]] |
| - | [[Category: Xuong, N | + | [[Category: Xuong, N H.]] |
[[Category: CMP]] | [[Category: CMP]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:46 2008'' |
Revision as of 10:10, 21 February 2008
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CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
Overview
BACKGROUND: Cyclic AMP binding domains possess common structural features yet are diversely coupled to different signaling modules. Each cAMP binding domain receives and transmits a cAMP signal; however, the signaling networks differ even within the same family of regulatory proteins as evidenced by the long-standing biochemical and physiological differences between type I and type II regulatory subunits of cAMP-dependent protein kinase. RESULTS: We report the first type II regulatory subunit crystal structure, which we determined to 2.45 A resolution and refined to an R factor of 0.176 with a free R factor of 0.198. This new structure of the type II beta regulatory subunit of cAMP-dependent protein kinase demonstrates that the relative orientations of the two tandem cAMP binding domains are very different in the type II beta as compared to the type I alpha regulatory subunit. Each structural unit for binding cAMP contains the highly conserved phosphate binding cassette that can be considered the "signature" motif of cAMP binding domains. This motif is coupled to nonconserved regions that link the cAMP signal to diverse structural and functional modules. CONCLUSIONS: Both the diversity and similarity of cAMP binding sites are demonstrated by this new type II regulatory subunit structure. The structure represents an intramolecular paradigm for the cooperative triad that links two cAMP binding sites through a domain interface to the catalytic subunit of cAMP-dependent protein kinase. The domain interface surface is created by the binding of only one cAMP molecule and is enabled by amino acid sequence variability within the peptide chain that tethers the two domains together.
About this Structure
1CX4 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit., Diller TC, Madhusudan, Xuong NH, Taylor SS, Structure. 2001 Jan 10;9(1):73-82. PMID:11342137
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