Fig. 2
From: Genetic insight into Birt–Hogg–Dubé syndrome in Indian patients reveals novel mutations at FLCN
FLCN exonic mutations and their effect on protein structure and interacting proteins. Green: N-terminal/Longin of FLCN, Brown: C-terminal of FLCN. Structures of homology modelled monomers of FLCN protein—(i) wild-type FLCN with amino-acid residues which were affected by mutations; (ii) stop-gain mutant FLCN affecting chain termination after Glu211 (i.e., p.Gln212*); (iii) indel (11-nucleotide) mutant FLCN affecting chain termination after Leu383 (i.e., p.Val384Phe*2); (iv) indel (single-nucleotide) mutant FLCN, altering the frame from His429 to Thr429, and subsequently creating a stop-codon after Leu435 in the model (i.e., p.His429Thr*39); (v) four-nucleotide duplicate mutant FLCN, altering the frame and terminating the chain after His442 in the model (i.e., p.Ala445Ser*11)