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Integrins

Integrin alphavbeta3 extracellular domains
PDB 1jv2 EBI.jpg
Structure of the extracellular segment of integrin alpha Vbeta3.
Identifiers
Symbol Integrin_alphaVbeta3
Pfam PF08441
Pfam clan CL0159
InterPro IPR013649
SCOP 1jv2
SUPERFAMILY 1jv2
Integrin alpha cytoplasmic region
PDB 1dpk EBI.jpg
Structure of chaperone protein PAPD.
Identifiers
Symbol Integrin_alpha
Pfam PF00357
InterPro IPR000413
PROSITE PDOC00215
SCOP 1dpk
SUPERFAMILY 1dpk
OPM superfamily 197
OPM protein 2knc
Integrin, beta chain
Integrinalpha.png
Identifiers
Symbol Integrin_beta
Pfam PF00362
InterPro IPR002369
SMART SM00187
PROSITE PDOC00216
SCOP 1jv2
SUPERFAMILY 1jv2
Integrin beta 7 cytoplasmic domain: complex with filamin
PDB 2brq EBI.jpg
crystal structure of the filamin a repeat 21 complexed with the integrin beta7 cytoplasmic tail peptide
Identifiers
Symbol Integrin_b_cyt
Pfam PF08725
InterPro IPR014836
SCOP 1m8O
SUPERFAMILY 1m8O

Integrins are transmembrane receptors that facilitate cell-extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allow rapid and flexible responses to events at the cell surface (i.e. signal platelets to initiate an interaction with coagulation factors).

Several types of integrins exist, and one cell may have multiple different types on its surface. Integrins are found in all animals.

Integrins work alongside other receptors such as cadherins, the immunoglobulin superfamily cell adhesion molecules, selectins and syndecans to mediate cell–cell and cell–matrix interaction. Ligands for integrins include fibronectin, vitronectin, collagen and laminin.

Integrins are obligate heterodimers, meaning that they have two subunits: α (alpha) and β (beta). Integrins in mammals have eighteen α and eight β subunits, in Drosophila five α and two β subunits, and in Caenorhabditis nematodes two α subunits and one β subunit. The α and β subunits each penetrate the plasma membrane and possess small cytoplasmic domains.

Variants of some subunits are formed by differential RNA splicing; for example, four variants of the beta-1 subunit exist. Through different combinations of the α and β subunits, around 24 unique integrins are generated.


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