Paxillin: Difference between revisions
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<StructureSection load='2vzi' size='400' side='right' caption='Human paxillin LD4 domain complex ( | <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 == | == 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. | '''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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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
*Paxillin (residues 1-20) | *Paxillin LD1 (residues 1-20) | ||
**[[4edn]] – hPXN + beta-parvin CH2 domain - human<br /> | **[[4edn]] – hPXN + beta-parvin CH2 domain - human<br /> | ||
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**[[4xgz]], [[4xh2]] – hPXN + antibody<br /> | **[[4xgz]], [[4xh2]] – hPXN + antibody<br /> | ||
**[[1ow8]], [[1ow7]] – hPXN + focal adhesion kinase focal adhesion targeting domain <br /> | **[[1ow8]], [[1ow7]] – hPXN + focal adhesion kinase focal adhesion targeting domain <br /> | ||
**[[5w93]] – mPXN + P130CAS - mouse<br /> | |||
*Paxillin LD4 (residues 20-41) | |||
**[[6iui]] – hPXN + GIT1 PBD domain<br /> | |||
*Paxillin (residues 139-162) | *Paxillin (residues 139-162) | ||
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**[[5uwh]] – hPXN + RAN + CRM1 + RANBP1<br /> | **[[5uwh]] – hPXN + RAN + CRM1 + RANBP1<br /> | ||
**[[3u3f]] – hPXN + tyrosine kinase PYK2 focal adhesion domain<br /> | **[[3u3f]] – hPXN + tyrosine kinase PYK2 focal adhesion domain<br /> | ||
**[[6jmu]] – mPXN + GIT1<br /> | |||
*Paxillin proline-rich region (residues 45-54) | *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
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3D structures of paxillin
Updated on 19-April-2026
