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2QFA

Crystal structure of a Survivin-Borealin-INCENP core complex

Summary for 2QFA
Entry DOI10.2210/pdb2qfa/pdb
DescriptorBaculoviral IAP repeat-containing protein 5, Borealin, Inner centromere protein, ... (6 entities in total)
Functional Keywordsthree-helical-bundle, long helix, protein complex, alternative splicing, apoptosis, cell cycle, cell division, centromere, chromosomal protein, cytoplasm, metal-binding, mitosis, nucleus, phosphorylation, polymorphism, protease inhibitor, thiol protease inhibitor, zinc, coiled coil, microtubule, cell cycle-cell cycle-cell cycle complex, cell cycle/cell cycle/cell cycle
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: O15392
Nucleus, nucleolus: Q53HL2
Chromosome, centromere: Q9NQS7
Total number of polymer chains3
Total formula weight29870.69
Authors
Jeyaprakash, A.A.,Klein, U.R.,Lindner, D.,Ebert, J.,Nigg, E.A.,Conti, E. (deposition date: 2007-06-27, release date: 2007-11-06, Last modification date: 2024-02-21)
Primary citationJeyaprakash, A.A.,Klein, U.R.,Lindner, D.,Ebert, J.,Nigg, E.A.,Conti, E.
Structure of a Survivin-Borealin-INCENP Core Complex Reveals How Chromosomal Passengers Travel Together.
Cell(Cambridge,Mass.), 131:271-285, 2007
Cited by
PubMed Abstract: The chromosomal passenger complex (CPC) is a key regulator of chromosome segregation and cytokinesis. CPC functions are connected to its localization. The complex first localizes to centromeres and later associates with the central spindle and midbody. Survivin, Borealin, and INCENP are the three components of the CPC that regulate the activity and localization of its enzymatic component, the kinase Aurora B. We determined the 1.4 A resolution crystal structure of the regulatory core of the CPC, revealing that Borealin and INCENP associate with the helical domain of Survivin to form a tight three-helical bundle. We used siRNA rescue experiments with structure-based mutants to explore the requirements for CPC localization. We show that the intertwined structural interactions of the core components lead to functional interdependence. Association of the core "passenger" proteins creates a single structural unit, whose composite molecular surface presents conserved residues essential for central spindle and midbody localization.
PubMed: 17956729
DOI: 10.1016/j.cell.2007.07.045
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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