Paxillin: Difference between revisions
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Michal Harel (talk | contribs) 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. | |||
== 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>. | ||
== 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 | *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 | *Paxillin LD4 (residues 20-41) | ||
**[[ | **[[6iui]] – hPXN + GIT1 PBD domain<br /> | ||
*Paxillin | *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 /> | ||
**[[2l6f]] – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR<br /> | **[[2l6f]] – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR<br /> | ||
**[[2vzi]] – hPXN + alpha-parvin C terminal <br /> | **[[2vzi]] – hPXN + alpha-parvin C terminal <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
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3D structures of paxillin
Updated on 19-April-2026