The interfaces of CHL4 (Cenp-N) C-terminal

Spot  🔔🔔🔔  for quick points

C-terminal accounts for 3 major and 1 minor interfaces of the whole Cenp-N 

Interfaces in action (Cenp-N residues are shown as spheres and corresponding protein residues as dots). Residues forming interfaces with both Cenp-O (cyan) and -P (violet) are marked in purple; Cenp-L (marine) and -O marked in light blue.

CHL4 (Cenp-N) interfaces with different subunits.

Subunits AME1 (Cenp-U), OKP1 (Cenp-Q) and NKP1 (Cenp-Y) interact with the N-terminal domain.

The C-terminal forms three major interfaces with IML3 (Cenp-L), MCM21 (Cenp-O) and CTF19 (Cenp-P). They account for 100% and 74% of the hydrogen bonds to Cenp-LN and COMA+ complexes,with a minimum buried surface area of 1300 Å2. The C-terminal appears to play a key role in the CCAN complex formation by strongly interacting with other subunits to form the Cenp-LN and COMA+ complexes. 

Although subunits MCM16 (Cenp-H) and NKP2 (Cenp-Z) interact with CHL4 C-terminal and N-terminal respectively, their interactions are not governed by hydrogen bonds nor salt bridges. 

🔔🔔🔔

C-terminal of CHL4 (Cenp-N) forms interfaces with IML3 (Cenp-L), MCM21 (Cenp-O), CTF19 (Cenp-P) and MCM16 (Cenp-H). Of which the first three are the largest interfaces, containing the highest numbers of hydrogen bonds and salt bridges.

 

➜ Interfaces up close

⇠ To recap the structure of CCAN

Prev Next