1ny3
From Proteopedia
(New page: 200px<br /> <applet load="1ny3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ny3, resolution 3.00Å" /> '''Crystal structure o...) |
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| - | [[Image:1ny3.gif|left|200px]]<br /> | + | [[Image:1ny3.gif|left|200px]]<br /><applet load="1ny3" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ny3" size=" | + | |
caption="1ny3, resolution 3.00Å" /> | caption="1ny3, resolution 3.00Å" /> | ||
'''Crystal structure of ADP bound to MAP KAP kinase 2'''<br /> | '''Crystal structure of ADP bound to MAP KAP kinase 2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the | + | MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the inflammatory process. We have determined the crystal structures of a catalytically active C-terminal deletion form of human MK2, residues 41-364, in complex with staurosporine at 2.7 A and with ADP at 3.2 A, revealing overall structural similarity with other Ser/Thr kinases. Kinetic analysis reveals that the K(m) for ATP is very similar for MK2 41-364 and p38-activated MK2 41-400. Conversely, the catalytic rate and binding for peptide substrate are dramatically reduced in MK2 41-364. However, phosphorylation of MK2 41-364 by p38 restores the V(max) and K(m) for peptide substrate to values comparable to those seen in p38-activated MK2 41-400, suggesting a mechanism for regulation of enzyme activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1NY3 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 ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NY3 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=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NY3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Federico, E.]] | [[Category: Federico, E.]] | ||
| - | [[Category: Hsiao, C | + | [[Category: Hsiao, C L.]] |
| - | [[Category: Kriz, R | + | [[Category: Kriz, R W.]] |
| - | [[Category: Lin, L | + | [[Category: Lin, L L.]] |
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: Maguire, M.]] | [[Category: Maguire, M.]] | ||
[[Category: Malakian, K.]] | [[Category: Malakian, K.]] | ||
[[Category: Mosyak, L.]] | [[Category: Mosyak, L.]] | ||
| - | [[Category: Parris, K | + | [[Category: Parris, K D.]] |
[[Category: Seehra, J.]] | [[Category: Seehra, J.]] | ||
[[Category: Shane, T.]] | [[Category: Shane, T.]] | ||
| - | [[Category: Somers, W | + | [[Category: Somers, W S.]] |
| - | [[Category: Stahl, M | + | [[Category: Stahl, M L.]] |
[[Category: Svenson, K.]] | [[Category: Svenson, K.]] | ||
[[Category: Taylor, M.]] | [[Category: Taylor, M.]] | ||
| - | [[Category: Telliez, J | + | [[Category: Telliez, J B.]] |
| - | [[Category: Underwood, K | + | [[Category: Underwood, K W.]] |
[[Category: Wolfrom, S.]] | [[Category: Wolfrom, S.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: ser/thr kinase]] | [[Category: ser/thr kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:16 2008'' |
Revision as of 12:11, 21 February 2008
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Crystal structure of ADP bound to MAP KAP kinase 2
Overview
MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the inflammatory process. We have determined the crystal structures of a catalytically active C-terminal deletion form of human MK2, residues 41-364, in complex with staurosporine at 2.7 A and with ADP at 3.2 A, revealing overall structural similarity with other Ser/Thr kinases. Kinetic analysis reveals that the K(m) for ATP is very similar for MK2 41-364 and p38-activated MK2 41-400. Conversely, the catalytic rate and binding for peptide substrate are dramatically reduced in MK2 41-364. However, phosphorylation of MK2 41-364 by p38 restores the V(max) and K(m) for peptide substrate to values comparable to those seen in p38-activated MK2 41-400, suggesting a mechanism for regulation of enzyme activity.
About this Structure
1NY3 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Catalytically active MAP KAP kinase 2 structures in complex with staurosporine and ADP reveal differences with the autoinhibited enzyme., Underwood KW, Parris KD, Federico E, Mosyak L, Czerwinski RM, Shane T, Taylor M, Svenson K, Liu Y, Hsiao CL, Wolfrom S, Maguire M, Malakian K, Telliez JB, Lin LL, Kriz RW, Seehra J, Somers WS, Stahl ML, Structure. 2003 Jun;11(6):627-36. PMID:12791252
Page seeded by OCA on Thu Feb 21 14:11:16 2008
Categories: Homo sapiens | Single protein | Federico, E. | Hsiao, C L. | Kriz, R W. | Lin, L L. | Liu, Y. | Maguire, M. | Malakian, K. | Mosyak, L. | Parris, K D. | Seehra, J. | Shane, T. | Somers, W S. | Stahl, M L. | Svenson, K. | Taylor, M. | Telliez, J B. | Underwood, K W. | Wolfrom, S. | ADP | Adp | Kinase | Map kap kinase 2 | Mk2 | Ser/thr kinase
