Paxillin
From Proteopedia
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| - | <StructureSection load='2vzi' size='340' side='right' caption='Human paxillin LD4 domain complex with | + | <StructureSection load='2vzi' size='340' side='right' caption='Human paxillin LD4 domain (grey) complex with α-parvin (green), tetraethylene glycol, triethylene glycol and etylene glycol (PDB code [[2vzi]])' scene=''> |
'''Paxillin''' (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). | '''Paxillin''' (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). | ||
== Function == | == Function == | ||
Revision as of 07:54, 21 October 2015
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3D structures of paxillin
Updated on 21-October-2015
