| 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
PXN serves as a docking protein recruiting signaling molecules to focal adhesions.
Disease
PXN has enhanced expression in several types of cancer PXN mutations are associated with lung cancer tumor growth.
Relevance
Structural highlights
PXN LD motifs are localized on the N-terminal region while the LIM double zinc finger domains are found at the C-terminal.
|
3D structures of paxillin
Updated on 21-October-2015
{"openlevels":0}
- Paxillin LD1 domain
- 4edn – hPXN + beta-parvin CH2 domain - human
- 2k2r – hPXN + beta-parvin CH2 domain - NMR
- 2vzg, 2vzd – hPXN + alpha-parvin C terminal
- 3rqe – hPXN + CCM3
- Paxillin LD2 domain
- 4xgz – hPXN + antibody
- 3u3f – hPXN + tyrosine kinase PYK2 focal adhesion domain
- 1ow8 – hPXN + focal adhesion kinase focal adhesion targeting domain
- 3rqf – hPXN + CCM3
- Paxillin LD4 domain
- 4r32 – cPXN + tyrosine kinase PYK2 focal adhesion targeting domain - chicken
- 1ow6, 3gm1 – hPXN + tyrosine kinase PYK2 focal adhesion targeting domain
- 1ow7 – hPXN + focal adhesion kinase focal adhesion targeting domain
- 2l6f – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR
- 4xh2 – hPXN + antibody
- 2vzi – hPXN + alpha-parvin C terminal
- 3rqg – hPXN + CCM3
- Paxillin proline-rich region
- 2o9v – hPXN + ponsin SH3 domain
References
