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Fig. 3 | BMC Ophthalmology

Fig. 3

From: Nanophthalmos patient with a THR518MET mutation in MYRF, a case report

Fig. 3

Analysis of MYRF variant, Thr518Met. a. Homology of MYRF sequences. Comparison of MYRF protein sequence from several organisms demonstrates that the threonine amino at position 518 is highly conserved across many species. Position 518 is indicated by red letters. Divergent amino acids are indicated by black background. b-e. Structural modeling of the Thr518Met MYRF variant. Beginning from an MYRF crystal structure, variant of residue 518 from Thr to Met followed by side-chain repacking demonstrates the loss of a canonical hydrogen-bond between Thr518 and Gln509 (1.9 Å) that stabilizes the interaction between two β-sheets within the MYRF DNA-binding domain (b and c). This suggests that a functional consequence of this variant is diminished folding stability, which may alter DNA-binding affinity and result in a reduction in transcriptional control. The mutant structure with a Met residue at position 518 (d and e) is surface exposed and can be accommodated without a substantial change in conformation

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