1iah: Difference between revisions

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[[Image:1iah.~~gif~~|left|200px]]

[[Image:1iah.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (ADP-MG COMPLEX)~~'''~~

===CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (ADP-MG COMPLEX)===

~~==Overview==~~

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Transient receptor potential (TRP) channels modulate calcium levels in eukaryotic cells in response to external signals. A novel transient receptor potential channel has the ability to phosphorylate itself and other proteins on serine and threonine residues. The ~~catalytic domain of~~ this ~~channel kinase has no detectable sequence similarity to classical eukaryotic protein kinases and is essential for channel function. The structure of the kinase domain~~, ~~reported here~~, ~~reveals unexpected similarity~~ to ~~eukaryotic protein kinases in~~ the ~~catalytic core~~ as ~~well as to metabolic enzymes with ATP-grasp domains~~. ~~The inclusion of the channel kinase catalytic domain within~~ the ~~eukaryotic protein kinase superfamily indicates a significantly wider distribution for this group of signaling proteins than suggested previously by sequence comparisons alone~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11389851}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11389851 is the PubMed ID number.

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==About this Structure==

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[[Category: Atp-grasp fold]]

[[Category: Protein kinase like fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:46:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:40:02 2008''

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-[[Image:1iah.gif|left|200px]]
+{{Seed}}
+[[Image:1iah.png|left|200px]]
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 {{STRUCTURE_1iah|  PDB=1iah  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (ADP-MG COMPLEX)'''
+===CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (ADP-MG COMPLEX)===
-==Overview==
+<!--
-Transient receptor potential (TRP) channels modulate calcium levels in eukaryotic cells in response to external signals. A novel transient receptor potential channel has the ability to phosphorylate itself and other proteins on serine and threonine residues. The catalytic domain of this channel kinase has no detectable sequence similarity to classical eukaryotic protein kinases and is essential for channel function. The structure of the kinase domain, reported here, reveals unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains. The inclusion of the channel kinase catalytic domain within the eukaryotic protein kinase superfamily indicates a significantly wider distribution for this group of signaling proteins than suggested previously by sequence comparisons alone.
+The line below this paragraph, {{ABSTRACT_PUBMED_11389851}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11389851 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11389851}}
 ==About this Structure==
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 [[Category: Atp-grasp fold]]
 [[Category: Protein kinase like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:46:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:40:02 2008''