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The structure reveals two residues (Pro228 and Ile276) which constitute a hydrophobic rigid binding surface for the acyl group of the ester and thus restricts the size of the acyl group that be accommodated.
One edge of the core β-sheet provides the extended binding surface for the NADP+ cofactor (as discussed further below).
PS provides a binding surface for the assembly of the coagulation tenase and prothrombinase complexes, which convert factor X into activated factor X (FXa) and prothrombin into thrombin, respectively [10], [11].
We speculate that disulphide bond formation between these residues alters the conformation of the B-helix such that it no longer forms a binding surface for the catalytic domain.
The first interface corresponds to the UIM binding surface and consists of residues K6, L8, I44, A46, G47, H68 and V70; the second interface corresponds to the binding surface for the VHS domain of STAM2 and consists of K11, I13, K27, K29, K33 and K63.
The Tower domain represents a binding surface for the LSD1 co-repressor partner protein CoREST [REST (RE1-silencing transcription factor) corepressor 1].
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In addition, the recent structural analysis of the binding surfaces for the 19S regulator both of the immuno- and constitutive 20S proteasome shows high similarity, such that the gating mechanisms for substrate entry are unlikely to differ (Huber et al., 2012).
Here, the first structure of a trypanosome receptor in complex with its ligand is presented: that of the T. brucei haptoglobin-haemoglobin receptor bound to haptoglobin-haemoglobin. Remarkably, the ligand-binding site extends more that half the way along the receptor, forming distinct binding surfaces for the β-subunit of haemoglobin and for haptoglobin.
One reasonable explanation of this observation can be that NHERF2 provides a common binding surface for both the ERM and the protein kinase which phosphorylates ERM.
In contrast, the DNA-binding surface for the lower-affinity structure is more neutral with disordered loops 1 3 disrupting positive patches observed in the Δ79AAG−εA T high-affinity complex.
Although the affinity of aS for CR is quite high, the binding surface for aS on the CR aggregates is small and limited to approximately one aS molecule per 60 CR molecules.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com