Abstract
Correction: Comparative Molecular Docking Analysis of Cytoplasmic Dynein Light Chain DYNLL1 with Pilin to Explore the Molecular Mechanism of Pathogenesis Caused by Pseudomonas aeruginosa PAO
Highlights
Cytoplasmic dynein is a part of large protein complex which functions as a minus-end directed microtubule based motor with the intermediate and light chains, doubtlessly entangled in the dynein binding to the appropriate cargo transport processes [1,2]
We identified that Pilin contains a homologous sequence (KSTQD) to DYNLL1 binding motif in its receptor binding domain (Figure 2)
The conservation pattern of this putative DYNLL1 interaction motif was studied in Pilin receptor binding domain across different strains of P. aeruginosa (PAO, KB7, PAK, CD4 and K122-4)
Summary
Cytoplasmic dynein is a part of large protein complex which functions as a minus-end directed microtubule based motor with the intermediate and light chains, doubtlessly entangled in the dynein binding to the appropriate cargo transport processes [1,2]. Human 8 kDa dynein light chain type 1 (DYNLL1) which was initially elucidated as a subunit of Chlamydomonas axonemal dynein [3], prevails in multiple functions. This light chain is found to be highly similar to a subset of mammal, nematode, insect, metazoan, plant, bacteria and yeast [4]. The short linear DYNLL1 interacting motifs are positioned in natively disordered protein segments [8] and exist near to the coiled-coil or other dimerization domains of the binding partners. DYNLL1 binding motifs are originally divided into two classes: K/R-XTQT or (K) X) T) Q0 T1 X2) and G-I/V-QVD or [X) G) (I/V))
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