1pi1
From Proteopedia
(New page: 200px<br /> <applet load="1pi1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pi1, resolution 2.0Å" /> '''Crystal structure of...) |
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| - | [[Image:1pi1.gif|left|200px]]<br /> | + | [[Image:1pi1.gif|left|200px]]<br /><applet load="1pi1" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pi1" size=" | + | |
caption="1pi1, resolution 2.0Å" /> | caption="1pi1, resolution 2.0Å" /> | ||
'''Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle pathways.'''<br /> | '''Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle pathways.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Mob protein family comprises a group of highly conserved eukaryotic | + | The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At the molecular level, Mob proteins act as kinase-activating subunits. We cloned a human Mob1 family member, Mob1A, and determined its three-dimensional structure by X-ray crystallography. The core of Mob1A consists of a four-helix bundle that is stabilized by a bound zinc atom. The N-terminal helix of the bundle is solvent exposed and together with adjacent secondary structure elements forms an evolutionarily conserved surface with a strong negative electrostatic potential. Several conditional mutant alleles of S. cerevisiae MOB1 target this surface and decrease its net negative charge. Interestingly, the kinases with which yeast Mob proteins interact have two conserved basic regions within their N-terminal lobe. Thus, Mob proteins may regulate their target kinases through electrostatic interactions mediated by conserved charged surfaces. |
==About this Structure== | ==About this Structure== | ||
| - | 1PI1 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PI1 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PI1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bothos, J.]] | [[Category: Bothos, J.]] | ||
| - | [[Category: Harris, K | + | [[Category: Harris, K G.]] |
[[Category: Huyen, Y.]] | [[Category: Huyen, Y.]] | ||
| - | [[Category: Jeffrey, P | + | [[Category: Jeffrey, P D.]] |
| - | [[Category: Luca, F | + | [[Category: Luca, F C.]] |
| - | [[Category: Pavletich, N | + | [[Category: Pavletich, N P.]] |
| - | [[Category: Stavridi, E | + | [[Category: Stavridi, E S.]] |
| - | [[Category: Stayrook, S | + | [[Category: Stayrook, S E.]] |
| - | [[Category: Voewerd, P | + | [[Category: Voewerd, P M.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dbf2]] | [[Category: dbf2]] | ||
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[[Category: mob1]] | [[Category: mob1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:56 2008'' |
Revision as of 12:29, 21 February 2008
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Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle pathways.
Overview
The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At the molecular level, Mob proteins act as kinase-activating subunits. We cloned a human Mob1 family member, Mob1A, and determined its three-dimensional structure by X-ray crystallography. The core of Mob1A consists of a four-helix bundle that is stabilized by a bound zinc atom. The N-terminal helix of the bundle is solvent exposed and together with adjacent secondary structure elements forms an evolutionarily conserved surface with a strong negative electrostatic potential. Several conditional mutant alleles of S. cerevisiae MOB1 target this surface and decrease its net negative charge. Interestingly, the kinases with which yeast Mob proteins interact have two conserved basic regions within their N-terminal lobe. Thus, Mob proteins may regulate their target kinases through electrostatic interactions mediated by conserved charged surfaces.
About this Structure
1PI1 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways., Stavridi ES, Harris KG, Huyen Y, Bothos J, Verwoerd PM, Stayrook SE, Pavletich NP, Jeffrey PD, Luca FC, Structure. 2003 Sep;11(9):1163-70. PMID:12962634
Page seeded by OCA on Thu Feb 21 14:28:56 2008
Categories: Homo sapiens | Single protein | Bothos, J. | Harris, K G. | Huyen, Y. | Jeffrey, P D. | Luca, F C. | Pavletich, N P. | Stavridi, E S. | Stayrook, S E. | Voewerd, P M. | ZN | Dbf2 | Mitosis | Mitotic exit network | Mob1
