Integrin
FunctionIntegrins (IG) are receptors which mediate the attachment between cells and between cells and the extracellular matrix. They are involved in cellular signaling and cell cycle[1]. IGs contain α and β chain. IG subunits span the cell membrane. Both subunits bind divalent cations some of which bind the ligands which interact with IG. Some IGs contain an insertion domain named I domain. For more details see Molecular Playground/IntegrinBeta1. For some details on the interaction of a targeting peptide with integrin see Molecular Playground/Targeting Peptide. DiseaseDefective integrin is the cause of the skin disease epidermolysis bullosa, of congenital muscular dystrophy. Overexpression of integrin is correlated with some types of cancer and enhanced bone resorption in osteoporosis[2]. Defective integrin is involved in periodontal diseases[3]. Structural highlightsThe interactions of integrin with ligands are dependent on the presence of divalent ions[4]. . Water molecules shown as red spheres. 3D structures of integrin |
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ReferencesReferences
- ↑ Humphries MJ. Integrin structure. Biochem Soc Trans. 2000;28(4):311-39. PMID:10961914
- ↑ Hillis GS, MacLeod AM. Integrins and disease. Clin Sci (Lond). 1996 Dec;91(6):639-50. PMID:8976799
- ↑ Larjava H, Koivisto L, Heino J, Hakkinen L. Integrins in periodontal disease. Exp Cell Res. 2014 Jul 15;325(2):104-10. doi: 10.1016/j.yexcr.2014.03.010. Epub, 2014 Mar 22. PMID:24662197 doi:http://dx.doi.org/10.1016/j.yexcr.2014.03.010
- ↑ Humphries MJ. Integrin structure. Biochem Soc Trans. 2000;28(4):311-39. PMID:10961914