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| - | [[Image:1xr1.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xr1| PDB=1xr1 | SCENE= }} | | {{STRUCTURE_1xr1| PDB=1xr1 | SCENE= }} |
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| - | '''Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution'''
| + | ===Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15525646}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15525646 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15525646}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: White, A.]] | | [[Category: White, A.]] |
| | [[Category: Protein kinase fold]] | | [[Category: Protein kinase fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:23:43 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:04:31 2008'' |
Revision as of 10:04, 27 July 2008
Template:STRUCTURE 1xr1
Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution
Template:ABSTRACT PUBMED 15525646
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 Sun Jul 27 13:04:31 2008
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Barringer, K. | Farmer, B. | Hickey, E R. | Kronkaitis, A. | Li, J. | Mische, S. | Peng, C. | Qian, K C. | Studts, J. | Wang, L. | White, A. | Protein kinase fold
