Annexin: Difference between revisions

No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(14 intermediate revisions by 2 users not shown)
Line 1: Line 1:
<StructureSection load='1n42' size='450' side='right' caption='Rat annexin V complex with Ca+2 (green) and sulfate (PDB code [[1n42]])' scene='41/410357/Cv/3'>
<StructureSection load='1n42' size='350' side='right' caption='Rat annexin V complex with Ca+2 (green) and sulfate (PDB code [[1n42]])' scene='41/410357/Cv/3'>
__TOC__
== Function ==
== Function ==


[[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat.  Annexins divide into species and are numbered from I to XII. '''Annexin V''' is the most abundant scaffolding protein. '''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. '''Annexin A-V''' has a major role in coagulation.  '''Annexin AII''' has a major role in fibrinolysis.  Annexins bind phospholipids and Ca+2 ions.
[[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat.  Annexins divide into species and are numbered from I to XII.
*'''Annexin I''' is involved in a variety of pathways<ref>PMID:17215481</ref>. <br />
*'''Annexin II''' is involved in angiogenesis, tutor progression and metastasis<ref>PMID:18220793</ref>. See also [[Ezetimibe]].<br /><br />
*'''Annexin V''' is the most abundant scaffolding protein. <br />
*'''Annexin VI''' is involved in endocytosis and regulates entry of ligands to prelysosomal compartment<ref>PMID:10940299</ref>. <br />
*'''Annexin VIII''' is calcium-dependent phospholipid-binding involved in blood coagulation<ref>PMID:8018923</ref>. <br />
*'''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. <br />
*'''Annexin A-V''' has a major role in coagulation.  <br />


== Relevance ==
== Relevance ==
Line 10: Line 18:
== Structural highlights ==
== Structural highlights ==


Annexins consist of 2 domains - the C-terminal core and the N-terminal head. The <scene name='41/410357/Cv/5'>core domain consists of 4 annexin repeats</scene> containing <scene name='41/410357/Cv/6'>5 helices</scene>. The core domain concave side contains the <scene name='41/410357/Cv/7'>Ca+2 binding sites</scene>.
Annexins consist of 2 domains - the C-terminal core and the N-terminal head. The <scene name='41/410357/Cv/9'>core domain consists of 4 annexin repeats</scene> containing <scene name='41/410357/Cv/10'>5 helices</scene>. The core domain concave side contains the <scene name='41/410357/Cv/11'>Ca+2 binding sites</scene>.<ref>PMID:12401794</ref>


==3D structures of annexin==
==3D structures of annexin==
 
[[Annexin 3D structures]]
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


* Annexin I
</StructureSection>


**[[2q4c]], [[1ycn]] - AnI - ''Arabidopsis thaliana''<br />
**[[1mcx]], [[1hm6]] - pAnI - pig<br />
**[[1qls]] - pAnI head+calgizzarrin<br />
**[[1bo9]] - hAnI head - human NMR<br />
**[[1ain]] - hAnI<br />
**[[4mdv]], [[4mdu]] – AnI + Ca – ''Schistosoma mansoni''<br />
* Annexin II
**[[2hyu]], [[2hyv]] - hAnII+heparin oligosaccharide<br />
**[[2hyw]], [[1xjl]] - hAnII+Ca<br />
**[[1w7b]] - hAnII<br />
**[[1bt6]] - hAnII head+calpactin light chain<br />
**[[4hre]] – AnII + protein S100-A10 + helicase-like transcription factor<br />
**[[4x9p]] – AnII – bovine<br />
* Annexin III
**[[1aii]], [[1axn]] - hAnIII<br />
* Annexin IV
**[[2zhi]], [[2zhj]], rAnIV+Na - rat<br />
**[[2zoc]] - hAnIV<br />
**[[1i4a]] - cAnIV (mutant) - cow<br />
**[[1aow]], [[1ann]] - cAnIV<br />
* Annexin V
**[[2ie6]], [[2ie7]], rAnV<br />
**[[1n41]], [[1n42]], [[1n44]], [[2h0k]], [[2h0l]], [[2h0m]], [[1bc0]], [[1bc1]], [[1bc3]], [[1bcw]], [[1bcy]], [[1bcz]]  - rAnV (mutant)<br />
**[[1g5n]] - rAnV+ heparin oligosaccharide<br />
**[[1a8a]], [[1a8b]] - rAnV+phospholipid analog<br />
**[[2ran]] - rAnV+Ca<br />
**[[1yii]] – chAnV+Ca – chicken<br />
**[[1yj0]] - chAnV+Zn<br />
**[[1ala]] - ChAnV<br />
**[[1hak]] - hAnV+K-201<br />
**[[1sav]] - hAnV (thioproline)<br />
**[[1hvd]], [[1hve]], [[1hvf]], [[1hvg]] - hAnV (mutant)<br />
**[[1anw]], [[1avh]], [[1avr]] - hAnV<br />
**[[1anx]] - hAnV+Ca<br />
**[[2xo2]] – hAnV + Ca + azidohomoalanine<br />
**[[2xo3]] - hAnV + Ca + homopropargylglycine
* Annexin VI
**[[1m9i]] - hAnVI (mutant)<br />
**[[1avc]] - cAnVI+Ca<br />
* Annexin VIII
**[[1w3w]] - hAnVIII<br />
**[[1w45]] - hAnVIII (mutant)<br />
* Annexin XII
**[[1dm5]] - HvAnXII (mutant) - ''Hydra vulgaris''<br />
**[[1aei]] - HvAnXII<br />
* Annexin E1
**[[3chj]] – GlAnE1 – ''Giardia lamblia''<br />
**[[3chk]], [[3chl]] – GlAnE1 + cation
* Other annexins
**[[1dk5]] - An24 - ''Capsicom annuum''<br />
**[[3brx]] - coAnGH1+Ca - cotton<br />
**[[1n00]] - coAnGH1<br />
}}


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Jaime Prilusky