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. 2011 May 13;8:35. doi: 10.1186/1742-4690-8-35

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Copyright ©2011 Bolin et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Structural modeling predicts that residue 186 lies near the end of the putative receptor binding cleft and influences packing of the conserved residue glutamine 110 (Q110). A. - B. The receptor binding domains of FeLV-A/61E (A) and FeLV-945 (B) were modeled using SwissModel and the molecular surfaces were calculated and drawn using 3D Molecule Viewer (Vector NTI, Invitrogen). Full views of the predicted surfaces are shown in white and a close up of the putative binding cleft (inset) is shown in cyan with residue 186 shown in green and residue 110 shown in magenta. C. Spacefilled depictions of residue 186 (green) and residue 110 (magenta) show the predicted difference in the position of Q110 between the SU of FeLV-A/61E and FeLV-945.