1jkk: Difference between revisions

Revision as of 14:23, 21 February 2008

2.4A X-RAY STRUCTURE OF TERNARY COMPLEX OF A CATALYTIC DOMAIN OF DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE AND MG.

OverviewOverview

We have determined X-ray crystal structures with up to 1.5 A resolution of the catalytic domain of death-associated protein kinase (DAPK), the first described member of a novel family of pro-apoptotic and tumor-suppressive serine/threonine kinases. The geometry of the active site was studied in the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The structures revealed a previously undescribed water-mediated stabilization of the interaction between the lysine that is conserved in protein kinases and the beta- and gamma-phosphates of ATP, as well as conformational changes at the active site upon ion binding. Comparison between these structures and nucleotide triphosphate complexes of several other kinases disclosed a number of unique features of the DAPK catalytic domain, among which is a highly ordered basic loop in the N-terminal domain that may participate in enzyme regulation.

About this StructureAbout this Structure

1JKK is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression., Tereshko V, Teplova M, Brunzelle J, Watterson DM, Egli M, Nat Struct Biol. 2001 Oct;8(10):899-907. PMID:11573098

Page seeded by OCA on Thu Feb 21 13:23:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1jkk.gif|left|200px]]<br />
+[[Image:1jkk.gif|left|200px]]<br /><applet load="1jkk" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1jkk" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1jkk, resolution 2.40&Aring;" />
 '''2.4A X-RAY STRUCTURE OF TERNARY COMPLEX OF A CATALYTIC DOMAIN OF DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE AND MG.'''<br />
 ==Overview==
-We have determined X-ray crystal structures with up to 1.5 A resolution of, the catalytic domain of death-associated protein kinase (DAPK), the first, described member of a novel family of pro-apoptotic and tumor-suppressive, serine/threonine kinases. The geometry of the active site was studied in, the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary, complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The, structures revealed a previously undescribed water-mediated stabilization, of the interaction between the lysine that is conserved in protein kinases, and the beta- and gamma-phosphates of ATP, as well as conformational, changes at the active site upon ion binding. Comparison between these, structures and nucleotide triphosphate complexes of several other kinases, disclosed a number of unique features of the DAPK catalytic domain, among, which is a highly ordered basic loop in the N-terminal domain that may, participate in enzyme regulation.
+We have determined X-ray crystal structures with up to 1.5 A resolution of the catalytic domain of death-associated protein kinase (DAPK), the first described member of a novel family of pro-apoptotic and tumor-suppressive serine/threonine kinases. The geometry of the active site was studied in the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The structures revealed a previously undescribed water-mediated stabilization of the interaction between the lysine that is conserved in protein kinases and the beta- and gamma-phosphates of ATP, as well as conformational changes at the active site upon ion binding. Comparison between these structures and nucleotide triphosphate complexes of several other kinases disclosed a number of unique features of the DAPK catalytic domain, among which is a highly ordered basic loop in the N-terminal domain that may participate in enzyme regulation.
 ==About this Structure==
-JKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JKK OCA].
+JKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKK OCA].
 ==Reference==
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 [[Category: Teplova, M.]]
 [[Category: Tereshko, V.]]
-[[Category: Watterson, D.M.]]
+[[Category: Watterson, D M.]]
 [[Category: ANP]]
 [[Category: MG]]
 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:41:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:40 2008''