Figure 1
Figure 1. Scheme of constructs and sequence alignment of the regions encompassing the furin motif of RGM proteins. (A) ClustalW alignment (http://www.ebi.ac.uk/clustalw)14 of human RGMs, showing amino acidic conservation 5′ and 3′ of the furin motif. RSER332NRR335 consensus sequence is boxed. The * above the boxed motif marks arginine 335. The degrees of conservation between proteins are indicated as follows: * indicates identical residue; :, conserved substitution; and ., semiconserved substitution. (B) From top to bottom, schematic representation of HJV functional domains in wild-type HJV and localization of the studied mutation (HJVR335Q) and chimeric variant (HJVKDEL). SP indicates signal peptide; RGD, arginine-glycine–aspartic acid integrin-binding domain; ◇, Cys residue; and ●, Asn residue. The dotted line indicates the autoproteolytic site. The double line shows the peptide used for the antibody production.

Scheme of constructs and sequence alignment of the regions encompassing the furin motif of RGM proteins. (A) ClustalW alignment (http://www.ebi.ac.uk/clustalw)14  of human RGMs, showing amino acidic conservation 5′ and 3′ of the furin motif. RSER332NRR335 consensus sequence is boxed. The * above the boxed motif marks arginine 335. The degrees of conservation between proteins are indicated as follows: * indicates identical residue; :, conserved substitution; and ., semiconserved substitution. (B) From top to bottom, schematic representation of HJV functional domains in wild-type HJV and localization of the studied mutation (HJVR335Q) and chimeric variant (HJVKDEL). SP indicates signal peptide; RGD, arginine-glycine–aspartic acid integrin-binding domain; ◇, Cys residue; and ●, Asn residue. The dotted line indicates the autoproteolytic site. The double line shows the peptide used for the antibody production.

Close Modal

or Create an Account

Close Modal
Close Modal