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1xqz

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[[Image:1xqz.jpg|left|200px]]<br /><applet load="1xqz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xqz.jpg|left|200px]]
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caption="1xqz, resolution 2.10&Aring;" />
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'''Crystal Structure of hPim-1 kinase at 2.1 A resolution'''<br />
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{{Structure
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|PDB= 1xqz |SIZE=350|CAPTION= <scene name='initialview01'>1xqz</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE= PIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of hPim-1 kinase at 2.1 A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1XQZ OCA].
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1XQZ 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=1XQZ OCA].
==Reference==
==Reference==
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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]
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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]]
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[[Category: protein kinase fold]]
[[Category: protein kinase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:24 2008''

Revision as of 13:13, 20 March 2008


PDB ID 1xqz

Drag the structure with the mouse to rotate
, resolution 2.10Å
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 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

1XQZ 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

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