Paxillin: Difference between revisions

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New page: <StructureSection load='1ow7' size='340' side='right' caption='Human paxillin LD4 domain complex with focal adhesion kinase focal adhesion targeting domain (PDB code 1ow7)' scene=''> ...
 
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<StructureSection load='2vzi' size='400' side='right' caption='Human paxillin LD4 domain complex (blue) with α-parvin (green), tetraethylene glycol, triethylene glycol and etylene glycol (PDB code [[2vzi]])' scene='71/715908/Cv/1' pspeed='8'>
== Function ==
'''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.


<StructureSection load='1ow7' size='340' side='right' caption='Human paxillin LD4 domain complex with focal adhesion kinase focal adhesion targeting domain (PDB code [[1ow7]])' 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 ==
PXN serves as a docking protein recruiting signaling molecules to focal adhesions.
== 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<ref>PMID:18172305</ref>.
== Relevance ==


== Structural highlights ==
== 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.  
PXN LD motifs are localized on the N-terminal region while the LIM double zinc finger domains are found at the C-terminal.  
 
*<scene name='71/715908/Cv/2'>Human paxillin LD4 domain interactions with α-parvin</scene>.
</StructureSection>
</StructureSection>


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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|


*Paxillin LD1 domain
*Paxillin LD1 (residues 1-20)


**[[4edn]] – hPXN + beta-parvin CH2 domain - human<br />
**[[4edn]] – hPXN + beta-parvin CH2 domain - human<br />
**[[2k2r]] – hPXN + beta-parvin CH2 domain - NMR<br />
**[[2k2r]] – hPXN + beta-parvin CH2 domain - NMR<br />
**[[2vzg]], [[2vzd]] – hPXN + alpha-parvin C terminal <br />
**[[2vzg]], [[2vzd]] – hPXN + alpha-parvin C terminal <br />
**[[3rqe]] – hPXN + CCM3<br />
**[[3rqe]], [[3rqg]], [[3rqf]] – hPXN + CCM3<br />
**[[1ow6]], [[3gm1]] – hPXN + tyrosine kinase PYK2 focal adhesion targeting domain <br />
**[[4xgz]], [[4xh2]] – hPXN + antibody<br />
**[[1ow8]], [[1ow7]] – hPXN + focal adhesion kinase focal adhesion targeting domain <br />
**[[5w93]] – mPXN + P130CAS - mouse<br />


*Paxillin LD2 domain
*Paxillin LD4 (residues 20-41)


**[[4xgz]] – hPXN + antibody<br />
**[[6iui]] – hPXN + GIT1 PBD domain<br />
**[[3u3f]] – hPXN + tyrosine kinase PYK2 focal adhesion domain<br />
**[[1ow8]] – hPXN + focal adhesion kinase focal adhesion targeting domain <br />
**[[3rqf]] – hPXN + CCM3<br />


*Paxillin LD4 domain
*Paxillin (residues 139-162)


**[[4r32]] – cPXN + tyrosine kinase PYK2 focal adhesion targeting domain - chicken<br />
**[[4r32]] – cPXN + tyrosine kinase PYK2 focal adhesion targeting domain - chicken<br />
**[[1ow6]], [[3gm1]] – hPXN + tyrosine kinase PYK2 focal adhesion targeting domain <br />
**[[1ow7]] – hPXN + focal adhesion kinase focal adhesion targeting domain <br />
**[[2l6f]] – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR<br />
**[[2l6f]] – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR<br />
**[[4xh2]] – hPXN + antibody<br />
**[[2vzi]] – hPXN + alpha-parvin C terminal <br />
**[[2vzi]] – hPXN + alpha-parvin C terminal <br />
**[[3rqg]] – hPXN + CCM3<br />


*Paxillin proline-rich region
*Paxillin (residues 260-281)
 
**[[5uwh]] – hPXN + RAN + CRM1 + RANBP1<br />
**[[3u3f]] – hPXN + tyrosine kinase PYK2 focal adhesion domain<br />
**[[6jmu]] – mPXN + GIT1<br />
 
*Paxillin proline-rich region (residues 45-54)


**[[2o9v]] – hPXN + ponsin SH3 domain<br />
**[[2o9v]] – hPXN + ponsin SH3 domain<br />
*Paxillin LIM3 domain (residues 380-499)
**[[7qb0]] – hPXN - NMR<br />
*Paxillin LIM4 domain (residues 527-591)
**[[6u4m]] – hPXN - NMR<br />
**[[6u4n]] – hPXN + kindling-2 - NMR<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

Latest revision as of 10:20, 19 April 2026

Human paxillin LD4 domain complex (blue) withα-parvin (green), tetraethylene glycol, triethylene glycol and etylene glycol (PDB code 2vzi)

Drag the structure with the mouse to rotate

3D structures of paxillin

Updated on 19-April-2026

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky