2IGP

Crystal Structure of Hec1 CH domain

Summary for 2IGP

• Entry DOI: 10.2210/pdb2igp/pdb
• Descriptor: Retinoblastoma-associated protein HEC, BETA-MERCAPTOETHANOL (3 entities in total)
• Functional Keywords: calponin homology (ch) domain, alpha helices, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O14777
• Total number of polymer chains: 1
• Total formula weight: 13956.28

Authors

Wei, R.R.,Harrison, S.C. (deposition date: 2006-09-22, release date: 2007-01-02, Last modification date: 2024-02-21)

Primary citation

Wei, R.R.,Al-Bassam, J.,Harrison, S.C.
The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment.
Nat.Struct.Mol.Biol., 14:54-59, 2007

PubMed Abstract: Kinetochores are multicomponent assemblies that connect chromosomal centromeres to mitotic-spindle microtubules. The Ndc80 complex is an essential core element of kinetochores, conserved from yeast to humans. It is a rod-like assembly of four proteins- Ndc80p (HEC1 in humans), Nuf2p, Spc24p and Spc25p. We describe here the crystal structure of the most conserved region of HEC1, which lies at one end of the rod and near the N terminus of the polypeptide chain. It folds into a calponin-homology domain, resembling the microtubule-binding domain of the plus-end-associated protein EB1. We show that an Ndc80p-Nuf2p heterodimer binds microtubules in vitro. The less conserved, N-terminal segment of Ndc80p contributes to the interaction and may be a crucial regulatory element. We propose that the Ndc80 complex forms a direct link between kinetochore core components and spindle microtubules.

PubMed: 17195848
DOI: 10.1038/nsmb1186

Experimental method

X-RAY DIFFRACTION (1.8 Å)