1xr1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xr1.gif|left|200px]]<br /><applet load="1xr1" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1xr1.gif|left|200px]]
-
caption="1xr1, resolution 2.10&Aring;" />
+
 
-
'''Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution'''<br />
+
{{Structure
 +
|PDB= 1xr1 |SIZE=350|CAPTION= <scene name='initialview01'>1xr1</scene>, resolution 2.10&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
 +
|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]
 +
|GENE= PIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1XR1 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]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XR1 OCA].
+
1XR1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XR1 OCA].
==Reference==
==Reference==
-
Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase., Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B, J Biol Chem. 2005 Feb 18;280(7):6130-7. Epub 2004 Nov 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15525646 15525646]
+
Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase., Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B, J Biol Chem. 2005 Feb 18;280(7):6130-7. Epub 2004 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15525646 15525646]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
Line 29: Line 38:
[[Category: protein kinase fold]]
[[Category: protein kinase fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:48 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:28 2008''

Revision as of 13:13, 20 March 2008


PDB ID 1xr1

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: and
Gene: PIM1 (Homo sapiens)
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution


Overview

Pim-1 kinase is a member of a distinct class of serine/threonine kinases consisting of Pim-1, Pim-2, and Pim-3. Pim kinases are highly homologous to one another and share a unique consensus hinge region sequence, ER-PXPX, with its two proline residues separated by a non-conserved residue, but they (Pim kinases) have <30% sequence identity with other kinases. Pim-1 has been implicated in both cytokine-induced signal transduction and the development of lymphoid malignancies. We have determined the crystal structures of apo Pim-1 kinase and its AMP-PNP (5'-adenylyl-beta,gamma-imidodiphosphate) complex to 2.1-angstroms resolutions. The structures reveal the following. 1) The kinase adopts a constitutively active conformation, and extensive hydrophobic and hydrogen bond interactions between the activation loop and the catalytic loop might be the structural basis for maintaining such a conformation. 2) The hinge region has a novel architecture and hydrogen-bonding pattern, which not only expand the ATP pocket but also serve to establish unambiguously the alignment of the Pim-1 hinge region with that of other kinases. 3) The binding mode of AMP-PNP to Pim-1 kinase is unique and does not involve a critical hinge region hydrogen bond interaction. Analysis of the reported Pim-1 kinase-domain structures leads to a hypothesis as to how Pim kinase activity might be regulated in vivo.

About this Structure

1XR1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase., Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B, J Biol Chem. 2005 Feb 18;280(7):6130-7. Epub 2004 Nov 3. PMID:15525646

Page seeded by OCA on Thu Mar 20 15:13:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools