1t4h

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|PDB= 1t4h |SIZE=350|CAPTION= <scene name='initialview01'>1t4h</scene>, resolution 1.80&Aring;
|PDB= 1t4h |SIZE=350|CAPTION= <scene name='initialview01'>1t4h</scene>, resolution 1.80&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|ACTIVITY= [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]
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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>
|GENE= PKRWNK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
|GENE= PKRWNK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4h OCA], [http://www.ebi.ac.uk/pdbsum/1t4h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t4h RCSB]</span>
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}}
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[[Category: wnk1]]
[[Category: wnk1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:13:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:51:12 2008''

Revision as of 20:51, 30 March 2008


PDB ID 1t4h

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Gene: PKRWNK1 (Rattus norvegicus)
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension


Overview

WNK kinases comprise a small group of unique serine/threonine protein kinases that have been genetically linked to pseudohypoaldosteronism type II, an autosomal dominant form of hypertension. Here we present the structure of the kinase domain of WNK1 at 1.8 A resolution, solved in a low activity conformation. A lysine residue (Lys-233) is found in the active site emanating from strand beta2 rather than strand beta3 as in other protein kinases. The activation loop adopts a unique well-folded inactive conformation. The conformations of the P+1 specificity pocket, the placement of the conserved active site threonine (Thr-386), and the exterior placement of helix C, contribute to the low activity state. By homology modeling, we identified two hydrophobic residues in the substrate-binding groove that contribute to substrate specificity. The structure of the WNK1 catalytic domain, with its unique active site, may help in the design of therapeutic reagents for the treatment of hypertension.

About this Structure

1T4H is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension., Min X, Lee BH, Cobb MH, Goldsmith EJ, Structure. 2004 Jul;12(7):1303-11. PMID:15242606

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