Corrigendum: Role of the CXCL13/CXCR5 axis in autoimmune diseases
Zijian Pan, Tong Zhu, Yanjun Liu, Nannan Zhang
Abstract
The N-terminal length and side-chain composition of CXCL13 affect crystallization, structure and 18 functional activity", and erroneously confused the protein structure of "Met CXCL13" with "wild 19 type (WT) CXCL13". In addition, we also mistakenly overlooked the presence of the signal peptide 20 in the CXCL13 precursor.A correction has been made to CXCL13/CXCR5 Protein Structure, paragraph 1: 22 "CXCL13 is a 109-amino-acid protein with a signal peptide of 22 amino acids, containing four 23 cysteine residues showing a C-X-C chemokine pattern (Figure 3A) (4). Typically, the tertiary 24 structure of chemokines is relatively conserved, consisting of a disordered N-terminal 'signaling 25 domain', followed by a 'core domain', which includes an 'N-loop', a 310-helix, a three-stranded β-