Paxillin
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3D structures of paxillin
Updated on 19-April-2026
FunctionPaxillin (PXN) is involved in actin membrane attachment at sites of cell adhesion to focal adhesion domains. PXN contains a number of domains which are involved in protein-protein interactions: LD, LIM, SH2 and SH3 binding sites. LD motifs are leucine-rich sequences which begin with leucine (L) and end with aspartate (D)[1]. PXN serves as a docking protein recruiting signaling molecules to focal adhesions. DiseasePXN has enhanced expression in several types of cancer. PXN mutations are associated with lung cancer tumor growth[2]. Structural highlightsPXN LD motifs are localized on the N-terminal region while the LIM double zinc finger domains are found at the C-terminal.
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Updated on 19-April-2026
This page was last modified 10:20, 19 April 2026.