2WJS

Crystal structure of the LG1-3 region of the laminin alpha2 chain

Summary for 2WJS

• Entry DOI: 10.2210/pdb2wjs/pdb
• Related: 1DYK 1OKQ 1QU0
• Descriptor: LAMININ SUBUNIT ALPHA-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: integrin, secreted, coiled coil, glycoprotein, laminin egf-like domain, extracellular matrix, laminin g-like domain, cell adhesion, disulfide bond, basement membrane
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 1
• Total formula weight: 68176.07

Authors

Carafoli, F.,Clout, N.J.,Hohenester, E. (deposition date: 2009-05-28, release date: 2009-06-23, Last modification date: 2024-11-13)

Primary citation

Carafoli, F.,Clout, N.J.,Hohenester, E.
Crystal Structure of the Lg1-3 Region of the Laminin {Alpha}2 Chain.
J.Biol.Chem., 284:22786-, 2009

PubMed Abstract: Laminins are large heterotrimeric glycoproteins with many essential functions in basement membrane assembly and function. Cell adhesion to laminins is mediated by a tandem of five laminin G-like (LG) domains at the C terminus of the alpha chain. Integrin binding requires an intact LG1-3 region, as well as contributions from the coiled coil formed by the alpha, beta, and gamma chains. We have determined the crystal structure at 2.8-A resolution of the LG1-3 region of the laminin alpha2 chain (alpha 2LG1-3). The three LG domains adopt typical beta-sandwich folds, with canonical calcium binding sites in LG1 and LG2. LG2 and LG3 interact through a substantial interface, but LG1 is completely dissociated from the LG2-3 pair. We suggest that the missing gamma chain tail may be required to stabilize the interaction between LG1 and LG2-3 in the biologically active conformation. A global analysis of N-linked glycosylation sites shows that the beta-sandwich faces of LG1 are free of carbohydrate modifications in all five laminin alpha chains, suggesting that these surfaces may harbor the integrin binding site. The alpha 2LG1-3 structure provides the first atomic view of the integrin binding region of laminins.

PubMed: 19553699
DOI: 10.1074/JBC.M109.026658

Experimental method

X-RAY DIFFRACTION (2.8 Å)