1pi1
From Proteopedia
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|PDB= 1pi1 |SIZE=350|CAPTION= <scene name='initialview01'>1pi1</scene>, resolution 2.0Å | |PDB= 1pi1 |SIZE=350|CAPTION= <scene name='initialview01'>1pi1</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Mob1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= Mob1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi1 OCA], [http://www.ebi.ac.uk/pdbsum/1pi1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pi1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Stayrook, S E.]] | [[Category: Stayrook, S E.]] | ||
[[Category: Voewerd, P M.]] | [[Category: Voewerd, P M.]] | ||
| - | [[Category: ZN]] | ||
[[Category: dbf2]] | [[Category: dbf2]] | ||
[[Category: mitosis]] | [[Category: mitosis]] | ||
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[[Category: mob1]] | [[Category: mob1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:53 2008'' |
Revision as of 19:59, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Mob1A (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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