Annexin
From Proteopedia
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[[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|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. <br /> | + | *'''Annexin I''' is involved in a variety of pathways<ref>PMID:17215481</ref>. <br /> |
| - | *'''Annexin V''' is the most abundant scaffolding | + | *'''Annexin V''' is the most abundant scaffolding protein. <br /> |
*'''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. <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 /> | *'''Annexin A-V''' has a major role in coagulation. <br /> | ||
Revision as of 09:43, 26 May 2024
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References
- ↑ Lim LH, Pervaiz S. Annexin 1: the new face of an old molecule. FASEB J. 2007 Apr;21(4):968-75. PMID:17215481 doi:10.1096/fj.06-7464rev
- ↑ Mo Y, Campos B, Mealy TR, Commodore L, Head JF, Dedman JR, Seaton BA. Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces. J Biol Chem. 2003 Jan 24;278(4):2437-43. Epub 2002 Oct 24. PMID:12401794 doi:10.1074/jbc.M210286200
