L, known as the human gene which functions ITGAL, in the immune system (lymphocyte function associated (P180), an antigen -1 antigens CD11a, and polypeptides) Further integrin. This is involved in co-stimulatory signaling and cell adhesion. This is the purpose of the drug efalizumab. ITGAL encodes the integrin L chain. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. To form a (LFA-1), combining beta 2 chain and (ITGB2) integrin lymphocyte function-associated antigen-1 expressed on all leukocytes This I-domain containing integrin alpha. Furthermore, (1-3 intercellular adhesion molecule) and its ligands, ICAMs 1-3, LFA-1 plays a central role in cell-cell leukocyte adhesion through interaction with functions of costimulatory signals of lymphocytes . With CD18 to form the lymphocyte function-associated antigen -1, CD11a, is one of the two components. The efalizumab act as immunosuppressants by binding to CD11a.

ITGAL encodes the integrin L chain. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. To form a (LFA-1), combining beta 2 chain and (ITGB2) integrin lymphocyte function-associated antigen-1 expressed on all leukocytes This I-domain containing integrin alpha. Furthermore, (1-3 intercellular adhesion molecule) and its ligands, ICAMs 1-3, LFA-1 plays a central role in cell-cell leukocyte adhesion through interaction with functions of costimulatory signals of lymphocytes . transcript variants encoding two different isoforms have been found for this gene.

Integrin adhesion is regulated through a process called “inside-out” signaling. To understand the molecular mechanisms of signaling inside-out integrin, we Mac-1 (αMβ2) or LFA-1 (αLβ2) mutations and express cytoplasmic domain that you have generated a cell line K562 stable. instead of the β2 domain cytoplasmic short additional film proximal 8 remaining, cutting, leading to αLβ2αMβ2, constitutive activation indicates the importance of membrane proximal region on the regulated integrin function adhesive. In addition, replacement of the cytoplasmic domain and the basic peptide and acidic and αLβ2 represent the α-helical coiled-coil was inactivated αLβ2. Association of the cytoplasmic domain these artificial revealed directly. On the other hand of the cytoplasmic domain and two peptides that do not form to activate αLβ2 αLβ2 and the α-helical coiled-coil, exchange. By activating the correlation of the cytoplasmic domain of mutation induction of activation of the epitope in the extracellular domain, introduction of the ligand binding. Cytoplasm of β integrin subunits limited between the integrin conformation α inert, our data indicate a close relationship film.

ITGAL encodes the integrin L chain. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. In order to form, in combination with beta-2 chain (ITGB2), and the I-domain containing integrin alpha -1 Antigen which is expressed on all leukocytes of integrin lymphocyte function-associated (LFA-1). Furthermore, (1-3 intercellular adhesion molecule) and its ligands, ICAMs 1-3, LFA-1 plays a central role in cell-cell leukocyte adhesion through interaction with functions of costimulatory signals of lymphocytes . transcript variants encoding two different isoforms have been found for this gene

Alpha-L/beta-2 integrin is a receptor for ICAM4 and ICAM1, ICAM2, ICAM3. Interaction of endothelial cells of leukocytes, cytotoxic T cell killing disease, and this is made from granulocytes and immune manifested in various ways, including antibody-dependent killing by monocytes
Integrin adhesion is regulated through a process called “inside-out” signaling. To understand the molecular mechanisms of signaling inside-out integrin, we Mac-1 (αMβ2) or LFA-1 (αLβ2) mutations and express cytoplasmic domain that you have generated a cell line K562 stable. instead of the β2 domain cytoplasmic short additional film proximal 8 remaining, cutting, leading to αLβ2αMβ2, constitutive activation indicates the importance of membrane proximal region on the regulated integrin function adhesive. In addition, replacement of the cytoplasmic domain and the basic peptide and acidic and αLβ2 represent the α-helical coiled-coil was inactivated αLβ2. Association of the cytoplasmic domain these artificial revealed directly. On the other hand of the cytoplasmic domain and two peptides that do not form to activate αLβ2 αLβ2 and the α-helical coiled-coil, exchange. By activating the correlation of the cytoplasmic domain of mutation induction of activation of the epitope in the extracellular domain, introduction of the ligand binding. Cytoplasm of β integrin subunits limited between the integrin conformation α inert, our data indicate a close relationship film.
structure of the I domain of integrin bound to the Ig superfamily of ligand αLβ2 is an example of the first interface and IgSF integrin ligand binding structure ICAM-1 is open. Mg2 of domain I is adjusted directly from -34 Glu of ICAM-1, I will allow for important salt bridge Glu-241 swing of domain residues dramatically. Ligand binding to indicate that it is likely to induce conformational changes in the allosteric signal and in αLI domain structure of the non-ligand and ligand binding, high, medium-affinity variants I domain intermediate without ligand You can be converted into a closed structure of the open conformation and. Close affinity is increased gradually, the dismantling of α7 C-terminal helix and the ratchet of disulfide bonds that were introduced in the β6-α7 loop in three different positions intermediate, in the open conformation.
Interaction of ICAM-1 ligand and cell adhesion molecules LFA-1 plays an important role in immune and inflammatory responses. Critical residues of ICAM-1 binding for LFA-1, are known as Domain I of β-subunit and I-domain α subunit. We investigated the activity, such as I-peptide domain binding mechanism CLAB of LBE that shows the inhibitory activity of the I domain cyclic peptide cLAB.L of LFA-1/ICAM-1 interaction here is based on the work of our previous. L. LBE cLAB.L has increased binding to epithelial cells and T cells. Adhesion of T cells to the epithelial monolayer, was inhibited by two peptides. I add the LBE in single layer in front of the inhibitory effect better addition cLAB.L result of the reverse. LBE, however cLAB.L the structure of ICAM-1, which means that it binds to ICAM-1 sites LBE is different cLAB.L, to generate improved structure of ICAM-1 for binding to CLAB I change the. L.