1a06

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(New page: 200px<br /><applet load="1a06" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a06, resolution 2.5&Aring;" /> '''CALMODULIN-DEPENDENT ...)
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'''CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT'''<br />
'''CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT'''<br />
==Overview==
==Overview==
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The crystal structure of calcium/calmodulin-dependent protein kinase I has, been determined in the autoinhibited form. The C-terminal regulatory, region of the enzyme forms a helix-loop-helix segment that extends across, the two domains of the catalytic core, making multiple inhibitory, interactions. Elements of the first regulatory alpha helix and the loop, interfere with the binding site for peptide substrates, while the loop and, the second helix interact with the ATP-binding domain to induce, conformational changes that obstruct the nucleotide binding pocket. One, part of the calmodulin recognition element protrudes away from the, catalytic domain and is potentially available for an initial interaction, with calmodulin. The structure provides a view of an intact calmodulin, target and suggests that substantial structural changes will accompany, kinase activation by calmodulin binding to the regulatory region.
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The crystal structure of calcium/calmodulin-dependent protein kinase I has been determined in the autoinhibited form. The C-terminal regulatory region of the enzyme forms a helix-loop-helix segment that extends across the two domains of the catalytic core, making multiple inhibitory interactions. Elements of the first regulatory alpha helix and the loop interfere with the binding site for peptide substrates, while the loop and the second helix interact with the ATP-binding domain to induce conformational changes that obstruct the nucleotide binding pocket. One part of the calmodulin recognition element protrudes away from the catalytic domain and is potentially available for an initial interaction with calmodulin. The structure provides a view of an intact calmodulin target and suggests that substantial structural changes will accompany kinase activation by calmodulin binding to the regulatory region.
==About this Structure==
==About this Structure==
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1A06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A06 OCA].
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1A06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A06 OCA].
==Reference==
==Reference==
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:31:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:27 2008''

Revision as of 09:39, 21 February 2008

Image:1a06.jpg

1a06, resolution 2.5Å

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CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT

Overview

The crystal structure of calcium/calmodulin-dependent protein kinase I has been determined in the autoinhibited form. The C-terminal regulatory region of the enzyme forms a helix-loop-helix segment that extends across the two domains of the catalytic core, making multiple inhibitory interactions. Elements of the first regulatory alpha helix and the loop interfere with the binding site for peptide substrates, while the loop and the second helix interact with the ATP-binding domain to induce conformational changes that obstruct the nucleotide binding pocket. One part of the calmodulin recognition element protrudes away from the catalytic domain and is potentially available for an initial interaction with calmodulin. The structure provides a view of an intact calmodulin target and suggests that substantial structural changes will accompany kinase activation by calmodulin binding to the regulatory region.

About this Structure

1A06 is a Single protein structure of sequence from Rattus norvegicus. Active as Calcium/calmodulin-dependent protein kinase, with EC number 2.7.11.17 Full crystallographic information is available from OCA.

Reference

Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I., Goldberg J, Nairn AC, Kuriyan J, Cell. 1996 Mar 22;84(6):875-87. PMID:8601311

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