Other ; This is the author accepted manuscript. The final version is available from Elsevier via http://dx.doi.org/10.1016/j.matbio.2016.08.010 ; Abstract ; The collagen-binding integrins recognise collagen through their inserted (I) domain, where co-ordination of a Mg$^{2+}$ ion in the metal ion-dependent site is reorganised by ligation by a collagen glutamate residue found in specific collagen hexapeptide motifs. Here we show that GROGER, found in the N-terminal domain of collagens I and III, is only weakly recognised by $α$10β1, an important collagen receptor on chondrocytes, contrasting with the other collagen-binding integrins. Alignment of I domain sequence and molecular modelling revealed a clash between a unique arginine residue (R215) in $α$10β1 and the positively-charged GROGER. Replacement of R215 with glutamine restored binding. Substituting arginine at the equivalent locus (Q214) in integrins $α$1 and $α$2 I domains impaired their binding to GROGER. Collagen II, abundant in cartilage, lacks GROGER. GRSGET is uniquely expressed in the C-terminus of collagen II, but this motif is similarly not recognised by $α$10β1. These data suggest an evolutionary imperative to maintain accessibility of the terminal domains of collagen II in tissues such as cartilage, perhaps during endochondral ossification, where $α$10β1 is the main collagen-binding integrin. ; Other ; This work was supported by British Heart Foundation programme grants, RG/15/4/31268 and RG/09/003/27122, and by a Wellcome Trust Biomedical Resource grant, 094470/Z/10/Z.