File:Mechanism for affinity switch in BMP-2 L100KN102D.tiff
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[edit]| Description | Figure 6. Mechanism for affinity switch in BMP-2 L100K/N102D. H-bond network around the conserved serine residue in Act-A (a), the BMP-2 variant L100K/N102D with increased ActR-IIB affinity (b) and wildtype BMP-2 (c). The conserved central H-bond between Ser88 Oγ (Ser90 in Act-A) and Leu61 amide of ActR-IIB is shown as green thick stippled line. The intramolecular H-bond network comprising Lys100, Asp102, Ser88 (Lys102, Asp104 and Ser90 in Act-A) and a nearby structurally conserved water molecule is indicated by stippled lines in magenta. The putative intermolecular H-bond between Lys102 of Act-A and Cys59 backbone carbonyl of ActR-IIB in the structure of the complex Act-A:ActR-IIBECD (PDB entry 1S4Y, [42]) is indicated by a thin line (a), as this H-bond is only present on one half of the dimeric complex and its geometrical parameters are close to exclusion cutoff criteria. A comparison of the position of the structurally conserved water molecule in the three structures shows that in wildtype BMP-2 (c) this solvent molecule is located directly above the central H-bond indicating direct accessibility of the H-bond by solvent. (d, e) Surface representation of ActR-IIB color coded by the contribution (ΔΔG in kJ mol-1) of each residue side chain to the binding free energy for (d) wildtype BMP-2 and (e) Act-A as measured by alanine scanning mutational analysis (see Table 1). For residue L61 the exchange to proline was used to point out the influence of the central conserved H-bond. The ΔΔG values are given in kJ mol-1. Dark red color marks hot spots of binding with an energy contribution of more than 15 kJ mol-1. Residues in yellow contribute only little; energy contribution of residues marked in blue is considered insignificant. |
| Date | |
| Source | https://bmcstructbiol.biomedcentral.com/articles/10.1186/1472-6807-7-6 Weber, D., Kotzsch, A., Nickel, J. et al. A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor. BMC Struct Biol 7, 6 (2007). https://doi.org/10.1186/1472-6807-7-6 |
| Author | Weber, D., Kotzsch, A., Nickel, J. et al. |
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| current | 18:35, 18 December 2024 |  | 1,947 × 1,366 (1.04 MB) | Rasbak (talk | contribs) | {{Information |description=Figure 6. Mechanism for affinity switch in BMP-2 L100K/N102D. H-bond network around the conserved serine residue in Act-A (a), the BMP-2 variant L100K/N102D with increased ActR-IIB affinity (b) and wildtype BMP-2 (c). The conserved central H-bond between Ser88 Oγ (Ser90 in Act-A) and Leu61 amide of ActR-IIB is shown as green thick stippled line. The intramolecular H-bond network comprising Lys100, Asp102, Ser88 (Lys102, Asp104 and Ser90 in Act-A) and a nearby struct... |
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