End-binding protein: Difference between revisions

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New page: <StructureSection load='2hkq' size='340' side='right' caption='Human end-binding protein 1 C terminal complex with dynactin (PDB code 2hkq)' scene=''> Updated on {{REVISIONDAY2}}-{{M...
 
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<StructureSection load='2hkq' size='340' side='right' caption='Human end-binding protein 1 C terminal (grey) complex with dynactin-1 CAP-GLY domain (green) (PDB code [[2hkq]])' scene=''>


<StructureSection load='2hkq' size='340' side='right' caption='Human end-binding protein 1 C terminal complex with dynactin (PDB code [[2hkq]])' scene=''>


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
'''End-binding protein''' or '''telomere-binding protein''' or '''microtubule-associated protein RP/EB family member''' (EB) regulates microtubules dynamics, promotes colony formation and enhances tumor growth.  EB is part of the proteins which accumulate at the growing microtubule plus end. During mitosis the EB associates with centrosome and spindle microtubules.  EB is involved in the regulation of chromosome stability and microtubule structure.  The C terminal domains of EB1 and EB3 are involved in dimer formation.  The CH (Calponin Homology) domain is an actin-binding domain<ref>PMID:11470413</ref>.  
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*'''End-binding protein 1''' accumulates at growing microtubule ends and regulates their dynamics<ref>PMID:28204846</ref>.
'''End-binding protein''' (EB) regulates microtubules dynamics, promotes colony formation and enhances tumor growth.  EB is part of the proteins which accumulate at the growing microtubule plus end. During mitosis the EB associates with centrosome and spindle microtubules.  EB is involved in the regulation of chromosome stability and microtubule structure.  The C terminal domains of EB1 and EB3 are involved in dimer formation.  The CH (Calponin Homology) domain is an actin-binding domain.  
*'''End-binding protein 2''' is involved in initial microtubule reorganization promoting stability and bundle formation<ref>PMID:23813963</ref>.
 
== Function ==
 
== Disease ==


== Relevance ==
== Structural highlights ==


</StructureSection>
</StructureSection>
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*End-binding protein 1 (MAPRE1)
*End-binding protein 1 (MAPRE1)
 
**[[1pa7]], [[1ueg]], [[1vka]], [[2r8u]] – hEB1 N terminal – human<br />
**[[1pa7]], [[1ueg]], [[1vka]], [[2r8u]] – hEB1 N terminal – human<br />
**[[1wu9]] – hEB1 C terminal <br />
**[[1wu9]] – hEB1 C terminal <br />
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**[[1txq]], [[2hkq]], [[2hl5]] – hEB1 C terminal + dynactin<br />
**[[1txq]], [[2hkq]], [[2hl5]] – hEB1 C terminal + dynactin<br />
**[[3gjo]] – hEB1 C terminal + dystonin<br />
**[[3gjo]] – hEB1 C terminal + dystonin<br />
**[[2qjz]] – hEB1 CH domain <br />
**[[2qjz]] – hEB1 CH domain 12-133<br />
**[[1v5k]] – EB1 CH domain (mutant) – mouse - NMR<br />
**[[5n74]] – hEB1 + KAR9 <br />
 
**[[9co5]] – hEB1 + FKBP12 <br />
**[[1v5k]] – mEB1 CH domain (mutant) – mouse - NMR<br />
**[[6evi]] – mEB1 C-terminal 191-260 - NMR<br />
**[[6evj]] – mEB1 C-terminal + modulator - NMR<br />
**[[7olg]] – mEB1 C-terminal + peptide - NMR<br />
**[[1k8g]], [[1kix]], [[1otc]], [[1ph1]], [[1ph2]], [[1ph3]], [[1ph4]], [[1ph5]], [[1ph6]], [[1ph7]], [[1ph8]], [[1ph9]], [[1phj]] – EB1 alpha+beta subunits + DNA – ''Sterkiella nova'' <br />
*End-binding protein 3
*End-binding protein 3
 
**[[3co1]] – hEB3 CH domain <br />
**[[3co1]] – hEB3 CH domain <br />
**[[1wyo]] – hEB3 CH domain - NMR<br />
**[[1wyo]] – hEB3 CH domain - NMR<br />
 
**[[3jak]], [[7sj9]] – hEB3 + tubulin – Cryo EM <br />
**[[9f3r]], [[9f3s]] – hEB3 + tubulin + GTP – Cryo EM <br />
**[[3jal]] – hEB3 + tubulin + GMPCPP – Cryo EM <br />
*End-binding protein 1+3
*End-binding protein 1+3
 
**[[3tq7]] – hEB3 C terminal + hEB1 C terminal + dynactin<br />
**[[3tq7]] – hEB3 C terminal + hEB1 C terminal + dynactin<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]