1mzk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mzk.gif|left|200px]]<br /><applet load="1mzk" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1mzk.gif|left|200px]]
-
caption="1mzk" />
+
 
-
'''NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis'''<br />
+
{{Structure
 +
|PDB= 1mzk |SIZE=350|CAPTION= <scene name='initialview01'>1mzk</scene>
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]
 +
|GENE= KAPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
 +
}}
 +
 
 +
'''NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1MZK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA].
+
1MZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA].
==Reference==
==Reference==
-
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase., Lee GI, Ding Z, Walker JC, Van Doren SR, Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14500786 14500786]
+
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase., Lee GI, Ding Z, Walker JC, Van Doren SR, Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14500786 14500786]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Phosphoprotein phosphatase]]
Line 20: Line 29:
[[Category: beta sandwich]]
[[Category: beta sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:37 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:50:14 2008''

Revision as of 10:50, 20 March 2008


PDB ID 1mzk

Drag the structure with the mouse to rotate
Gene: KAPP (Arabidopsis thaliana)
Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16
Coordinates: save as pdb, mmCIF, xml



NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis


Overview

Forkhead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with high precision and accuracy using residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology only in the recognition loops, this fold is shared with FHA domains from checkpoint proteins from yeast and humans, as well as with nonhomologous MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity throughout FHA domains and Smad MH2 domains may stabilize the core of the beta-sandwich. Evolutionary trace analysis of FHA domains suggests class-specific residues in the recognition loops that could tune their phosphoprotein-binding specificity. This surface agrees with that of KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary trace analysis also predicts an unexpected swath of class-specific residues on another face of FHA domains. Protein interactions with these faces may affect assembly of transmembrane signaling complexes in plants, and in other FHA domain-containing assemblies.

About this Structure

1MZK is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase., Lee GI, Ding Z, Walker JC, Van Doren SR, Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:14500786

Page seeded by OCA on Thu Mar 20 12:50:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools