Molecular modeling of the C1q domain of otolin. YangHua ZhaoXing XuYinfang WangLili HeQuanyuan Wang LundbergYunxia 2011 <p>(<b>A</b>) The tertiary structures of Col10a1-C1q domain (green) and otolin-C1q domain (magenta) are nearly super-imposable. The modeled structure is consistent with the crystal structure of human COL10A1. Ca<sup>2+</sup>-binding residues are labeled and projected as sticks. (<b>B</b>) The surface of the otolin-C1q domain with temperature factors denoted in different colors. (<b>C</b>) Clustering of residues and the cationic surface of otolin-C1q domain. Residues are colored according to their electrical charges and hydrophobic nature. The nine key cationic residues are labeled and projected as sticks. (<b>D</b>) The protein backbone RMSD during 1ns simulation. After 400ps, the structure is stable. The 400–1000 ps range was used for computing the final structure. (<b>E</b>) The temperature factor (RMS fluctuation) of each residue. The residues with higher RMS fluctuation usually are exposed on molecule surface and may construct active sites. The Ca<sup>2+</sup>-binding residues in (A) are labeled.</p>