Integrin beta 7

Structure

Like all integrin subunits, β is a highly flexible, membrane-bound, extracellular protein that must pair with an α subunit for stability. The molecule's flexibility allows it to dynamically regulate its affinity for ligand through conformational changes. Beginning with the apical end of the protein, farthest from the cell membrane, the β is composed of a head and upper legs, collectively known as the headpiece, lower legs, a transmembrane domain and a cytoplasmic tail. The top of the head is the I-like domain, sometimes called the βI domain, which, in combination with the α subunit, binds ligand. Just below this is the hybrid domain, a portion of which is N-terminal to the I-like domain. Below the hybrid domain is the PSI domain, which completes the headpiece. The lower legs consist of EGF domains 1-4 and the β tail domain. Finally there is a transmembrane domain, and the C-terminal cytoplasmic tail.

Interactions

ITGB7 has been shown to interact with EED.

References

References

1. (Jun 1991). "Complete amino acid sequence of an integrin beta subunit (beta 7) identified in leukocytes". The Journal of Biological Chemistry.
2. "Entrez Gene: ITGB7 integrin, beta 7".
3. (Nov 2009). "Anti-integrin monoclonal antibodies". Journal of Cell Science.
4. (Oct 2003). "Integrin avidity regulation: are changes in affinity and conformation underemphasized?". Current Opinion in Cell Biology.
5. (Jan 2012). "Structural specializations of α(4)β(7), an integrin that mediates rolling adhesion". The Journal of Cell Biology.
6. (Oct 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". The Journal of Biological Chemistry.