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Paxillin
From Proteopedia
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<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=''> | <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). | ||
== Function == | == Function == | ||
| - | PXN serves as a docking protein recruiting signaling molecules to focal adhesions. | + | '''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)<ref>PMID:11911889</ref>. PXN serves as a docking protein recruiting signaling molecules to focal adhesions. |
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== Disease == | == Disease == | ||
PXN has enhanced expression in several types of cancer PXN mutations are associated with lung cancer tumor growth. | PXN has enhanced expression in several types of cancer PXN mutations are associated with lung cancer tumor growth. | ||
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== Relevance == | == Relevance == | ||
Revision as of 08:59, 15 June 2016
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3D structures of paxillin
Updated on 15-June-2016
