1JLM
I-DOMAIN FROM INTEGRIN CR3, MN2+ BOUND
Summary for 1JLM
| Entry DOI | 10.2210/pdb1jlm/pdb |
| Descriptor | INTEGRIN, MANGANESE (II) ION (3 entities in total) |
| Functional Keywords | integrin, cell adhesion protein, glycoprotein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : P11215 |
| Total number of polymer chains | 1 |
| Total formula weight | 22049.05 |
| Authors | Lee, J.-O.,Liddington, R. (deposition date: 1996-04-09, release date: 1997-01-11, Last modification date: 2024-05-22) |
| Primary citation | Lee, J.O.,Bankston, L.A.,Arnaout, M.A.,Liddington, R.C. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure, 3:1333-1340, 1995 Cited by PubMed Abstract: Integrins are plasma membrane proteins that mediate adhesion to other cells and to components of the extracellular matrix. Most integrins are constitutively inactive in resting cells, but are rapidly and reversibly activated in response to agonists, leading to highly regulated cell adhesion. This activation is associated with conformational changes in their extracellular portions, but the nature of the structural changes that lead to a change in adhesiveness is not understood. The interactions of several integrins with their extracellular ligands are mediated by an A-type domain (generally called the I-domain in integrins). Binding of the I-domain to protein ligands is dependent on divalent cations. We have described previously the structure of the I-domain from complement receptor 3 with bound Mg2+, in which the glutamate side chain from a second I-domain completes the octahedral coordination sphere of the metal, acting as a ligand mimetic. PubMed: 8747460DOI: 10.1016/S0969-2126(01)00271-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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