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Domain-domain interactions involve the binding of two globular domains from different proteins, thereby creating a large contact interface of 2.000Å2 [5] on average.
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The structure of CaM consists of two globular calcium-binding domains joined by a central 28-residue alpha helix.
The molecule consists of two globular lobes connected by a long exposed alpha-helix.
IgG is composed of three globular domain structures, two of which are the fragments for antigen binding (Fab) and the other is the fragment crystalizable (Fc) that activates Fcγ receptors (FcγRs) on leukocytes and C1 component of complement.
The protein is composed of four globular domains.
The aggrecan molecule consists of three globular domains, two chondroitin sulfate domains, and one keratin region.
Additionally, the electric surface potential landscape at the target protein binding regions on the two globular domains of hCLP is significantly different from those of CaM, indicating that the respective ranges of hCLP and hCaM target proteins do not fully overlap.
The main consequence of the mutation is a change in the relative orientation of the two globular calcium-binding domains, causing the hydrophobic patches in these domains to be closer and much less accessible to interact with the target enzymes.
The structures of these two globular domains have been solved in human RAP30 [ 68, 69].
The two globular domains of Sirt3 composed of an NAD binding Rossmann fold and a zinc binding motif are similar to other sirtuins (Avalos et al., 2004; Du et al., 2011; Yuan and Marmorstein, 2012; Jiang et al., 2013).
TnC senses Ca2+ through up to four Ca2+ binding motifs (EF-hands) distributed across two globular domains, the N- and C-terminal domains (7− 11).
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