Structural Analysis based on examples

 

1) CTF19:MCM21 interface .

 

 From previous exhibit (👈Click it!), it is known that hydrogen bonds and salt bridges in CTF19:MCM21 interface are highly conserved which contribute to high binding affinity while Van der Waals interactions only contribute in a large quantity.

 

 CTF19:MCM21 motif was firstly identified as one complex and co-expressed in COMA assembly in previous studies. It functions as a branch for the assembly of related inner kinetochore subunits and is essential for accurate chromosome segregagion1.The high binding affinity between CTF19:MCM21 ensures its normal biological function.

CTF19-MCM21 bonding interactions

The color magenta shows chain CTF19 and cyan represents the chain MCM21. Hydrogen bonds, salt bridges and non-bonded contacts are shown in yellow, green and orange respectively.

Binding affinity and number of interactions of CTF19:MCM21 interface

2) CTF19:CTF3 interface .

 CTF19:CTF3 complex shows low binding affinity without any hydrogen bond or salt bridge.

 Most of the residues involved in Van der Waals interactions have a low conservation degree (for more information click👉previous exihibit), indicating that merely forming Van Der Waals interactions is not enough to generate strong protein-protein binding.

CTF19-CTF3 bonding interactions

The color magenta shows chain CTF19 and palegreen represents the chain CTF3. Salt bridges are shown in orange.

Binding affinity and number of interactions of CTF19:CTF3 interface

Reference

1.        Schmitzberger F, Richter MM, Gordiyenko Y, Robinson C V, Dadlez M, Westermann S.  Molecular basis for inner kinetochore configuration through RWD domain–peptide interactions . EMBO J. 2017;36(23):3458-3482. doi:10.15252/embj.201796636

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