1ZON

CD11A I-DOMAIN WITHOUT BOUND CATION

Summary for 1ZON

• Entry DOI: 10.2210/pdb1zon/pdb
• Descriptor: LEUKOCYTE ADHESION GLYCOPROTEIN (2 entities in total)
• Functional Keywords: integrin, cell adhesion, glycoprotein, transmembrane, extracellular matrix, cytoskeleton
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P20701
• Total number of polymer chains: 1
• Total formula weight: 21323.49

Authors

Leahy, D.J.,Qu, A. (deposition date: 1996-06-20, release date: 1996-12-07, Last modification date: 2024-02-14)

Primary citation

Qu, A.,Leahy, D.J.
The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin.
Structure, 4:931-942, 1996

PubMed Abstract: The integrin family of cell-surface receptors mediates a wide variety of cell-cell and cell-extracellular matrix interactions. Integrin-ligand interactions are invariably dependent on the presence of divalent cations, and a subset of integrins contain a approximately 200 amino acid inserted (I) domain that is important for ligand binding activity and contains a single divalent cation binding site. Many integrins are believed to respond to stimuli by undergoing a conformational change that increases their affinity for ligand, and there is a clear difference between two crystal structures of the CD11b I domain with different divalent cations (magnesium and manganese) bound. In addition to the different bound cation, a 'ligand mimetic' crystal lattice interaction in the CD11b I domain structure with bound magnesium has led to the interpretation that the different CD11b I domain structures represent different affinity states of I domains. The influence of the bound cation on I domain structure and function remains incompletely understood, however. The crystal structure of the CD11a I domain bound to manganese is known. We therefore set out to determine whether this structure changes when the metal ion is altered or removed.

PubMed: 8805579
DOI: 10.1016/S0969-2126(96)00100-1

Experimental method

X-RAY DIFFRACTION (2 Å)