1ian: Difference between revisions

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[[Image:1ian.gif|left|200px]]<br />

[[Image:1ian.gif|left|200px]]<br /><applet load="1ian" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1ian" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ian, resolution 2.0Å" />

'''HUMAN P38 MAP KINASE INHIBITOR COMPLEX'''<br />

==Overview==

The crystal structure of human p38 mitogen-activated protein (MAP) kinase, in complex with a potent and highly specific pyridinyl-imidazole inhibitor, has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the, closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A, hydrogen bond is made between the pyridyl nitrogen of the inhibitor and, the main chain amido nitrogen of residue 109, analogous to the interaction, from the N1 atom of ATP. The crystal structure provides possible, explanations for the specificity of this class of inhibitors. Other, protein kinase inhibitors may achieve their specificity through a similar, mechanism. The structure also reveals a possible second binding site for, this inhibitor, with currently unknown function.

The crystal structure of human p38 mitogen-activated protein (MAP) kinase in complex with a potent and highly specific pyridinyl-imidazole inhibitor has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A hydrogen bond is made between the pyridyl nitrogen of the inhibitor and the main chain amido nitrogen of residue 109, analogous to the interaction from the N1 atom of ATP. The crystal structure provides possible explanations for the specificity of this class of inhibitors. Other protein kinase inhibitors may achieve their specificity through a similar mechanism. The structure also reveals a possible second binding site for this inhibitor, with currently unknown function.

==About this Structure==

1IAN 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 D13 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IAN OCA].

1IAN 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=D13:'>D13</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAN OCA].

==Reference==

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[[Category: serine/threonine-protein kinase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:28:~~04 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:46 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ian.gif|left|200px]]<br />
+[[Image:1ian.gif|left|200px]]<br /><applet load="1ian" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ian" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ian, resolution 2.0&Aring;" />
 '''HUMAN P38 MAP KINASE INHIBITOR COMPLEX'''<br />
 ==Overview==
-The crystal structure of human p38 mitogen-activated protein (MAP) kinase, in complex with a potent and highly specific pyridinyl-imidazole inhibitor, has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the, closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A, hydrogen bond is made between the pyridyl nitrogen of the inhibitor and, the main chain amido nitrogen of residue 109, analogous to the interaction, from the N1 atom of ATP. The crystal structure provides possible, explanations for the specificity of this class of inhibitors. Other, protein kinase inhibitors may achieve their specificity through a similar, mechanism. The structure also reveals a possible second binding site for, this inhibitor, with currently unknown function.
+The crystal structure of human p38 mitogen-activated protein (MAP) kinase in complex with a potent and highly specific pyridinyl-imidazole inhibitor has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A hydrogen bond is made between the pyridyl nitrogen of the inhibitor and the main chain amido nitrogen of residue 109, analogous to the interaction from the N1 atom of ATP. The crystal structure provides possible explanations for the specificity of this class of inhibitors. Other protein kinase inhibitors may achieve their specificity through a similar mechanism. The structure also reveals a possible second binding site for this inhibitor, with currently unknown function.
 ==About this Structure==
-IAN 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 D13 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAN OCA].
+IAN 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=D13:'>D13</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAN OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: serine/threonine-protein kinase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:28:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:46 2008''