《Table 2 Side chain modifications and their effects on CXCL12α》

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《The unique structural and functional features of CXCL12》

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Abbreviations:ND，not determined；N-Tyr，nitrotyrosine.

After controlled transcription and translation，CXCL12 activity is further regulated posttranslationally through enzymatic or chemical modifications.These changes alter several aspects of CXCL12，including GAG-binding properties and receptor binding and activation.The modifications that have been detected to occur are NH2-terminal and COOH-terminal truncation，citrullination of Arg residues and nitration of Tyr residues.The modified amino acids and the responsible agents are listed in Tables 1 and 2 and are indicated on the amino acid sequence of CXCL12 shown in Figure 1a.To appreciate the localization of these amino acids in the tertiary structure of CXCL12，the modified amino acids are also highlighted in a 3D model of the chemokine in Figure 1b.