1duj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1duj.jpg|left|200px]] | [[Image:1duj.jpg|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2''' | {{Structure | ||
|PDB= 1duj |SIZE=350|CAPTION= <scene name='initialview01'>1duj</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1DUJ is a [ | 1DUJ 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=1DUJ OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20., Luo X, Fang G, Coldiron M, Lin Y, Yu H, Kirschner MW, Wagner G, Nat Struct Biol. 2000 Mar;7(3):224-9. PMID:[http:// | Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20., Luo X, Fang G, Coldiron M, Lin Y, Yu H, Kirschner MW, Wagner G, Nat Struct Biol. 2000 Mar;7(3):224-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10700282 10700282] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: spindle assembly checkpoint]] | [[Category: spindle assembly checkpoint]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:35 2008'' | ||
Revision as of 11:44, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2
OverviewOverview
The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate. We report the solution structure of human Mad2 and its interaction with Cdc20. Mad2 possesses a novel three-layered alpha/beta fold with three alpha-helices packed between two beta-sheets. Using deletion mutants we identified the minimal Mad2-binding region of human Cdc20 as a 40-residue segment immediately N-terminal to the WD40 repeats. Mutagenesis and NMR titration experiments show that a C-terminal flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20 form a tight 1:1 heterodimeric complex in which the C-terminal segment of Mad2 becomes folded. These results provide the first structural insight into mechanisms of the spindle assembly checkpoint.
About this StructureAbout this Structure
1DUJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20., Luo X, Fang G, Coldiron M, Lin Y, Yu H, Kirschner MW, Wagner G, Nat Struct Biol. 2000 Mar;7(3):224-9. PMID:10700282
Page seeded by OCA on Thu Mar 20 10:44:35 2008