1ll8

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[[Image:1ll8.gif|left|200px]]
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{{Structure
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|PDB= 1ll8 |SIZE=350|CAPTION= <scene name='initialview01'>1ll8</scene>
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The line below this paragraph, containing "STRUCTURE_1ll8", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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{{STRUCTURE_1ll8| PDB=1ll8 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://www.ebi.ac.uk/pdbsum/1ll8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB]</span>
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'''Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation'''
'''Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation'''
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[[Category: Harper, S M.]]
[[Category: Harper, S M.]]
[[Category: Rutter, J.]]
[[Category: Rutter, J.]]
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[[Category: kinase regulation]]
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[[Category: Kinase regulation]]
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[[Category: ligand binding]]
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[[Category: Ligand binding]]
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[[Category: ligand screening]]
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[[Category: Ligand screening]]
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[[Category: pas domain]]
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[[Category: Pas domain]]
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Revision as of 21:01, 2 May 2008

Template:STRUCTURE 1ll8

Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation


Overview

PAS domains are sensory modules in signal-transducing proteins that control responses to various environmental stimuli. To examine how those domains can regulate a eukaryotic kinase, we have studied the structure and binding interactions of the N-terminal PAS domain of human PAS kinase using solution NMR methods. While this domain adopts a characteristic PAS fold, two regions are unusually flexible in solution. One of these serves as a portal that allows small organic compounds to enter into the core of the domain, while the other binds and inhibits the kinase domain within the same protein. Structural and functional analyses of point mutants demonstrate that the compound and ligand binding regions are linked, suggesting that the PAS domain serves as a ligand-regulated switch for this eukaryotic signaling system.

About this Structure

1LL8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation., Amezcua CA, Harper SM, Rutter J, Gardner KH, Structure. 2002 Oct;10(10):1349-61. PMID:12377121 Page seeded by OCA on Sat May 3 00:01:56 2008

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