integrin alphaX-beta2 complex

Definition

Target type: cellularcomponent

An integrin complex that comprises one alphaX subunit and one beta2 subunit. [PMID:12297042]

The integrin alphaX-beta2 complex, also known as CD11c/CD18 or Mac-1, is a heterodimeric transmembrane receptor expressed primarily on leukocytes. It plays a critical role in leukocyte adhesion, migration, and signaling. The cellular component of this complex can be described as follows:

- **Extracellular domain:** The extracellular domain of the complex consists of two subunits, alphaX (CD11c) and beta2 (CD18), each containing multiple domains. The alphaX subunit has an I domain, a beta-propeller domain, a thigh domain, a calf-1 domain, a calf-2 domain, and a transmembrane domain. The beta2 subunit comprises a beta-propeller domain, a PSI domain, a hybrid domain, a transmembrane domain, and a cytoplasmic tail. The I domain of alphaX mediates binding to specific ligands, such as iC3b, fibrinogen, and ICAM-1.
- **Transmembrane domain:** The transmembrane domains of both alphaX and beta2 subunits anchor the complex to the plasma membrane. These domains are characterized by hydrophobic amino acid residues that interact with the lipid bilayer.
- **Cytoplasmic domain:** The cytoplasmic domains of alphaX and beta2 subunits play a crucial role in signal transduction. The beta2 subunit cytoplasmic domain interacts with various intracellular signaling molecules, including talin, kindlin, and PI3K. These interactions facilitate the activation of downstream signaling pathways involved in cell adhesion, migration, and activation.

Overall, the cellular component of integrin alphaX-beta2 complex is a highly complex structure with multiple domains and interacting partners. These features allow for the versatile functions of this receptor in leukocyte biology.'
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Proteins (1)

Compounds (11)