1L5G

CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND

Summary for 1L5G

• Entry DOI: 10.2210/pdb1l5g/pdb
• Related: 1JV2
• Descriptor: INTEGRIN ALPHA V, INTEGRIN BETA-3, CYCLIC ARG-GLY-ASP PEPTIDE, ... (7 entities in total)
• Functional Keywords: genu, hybrid domain, beta-tail domain, psi domain, egf domain, midas, admidas, limbs, cage motif, propeller, a-domain, thigh domain, calf domain, rgd ligand, cell adhesion
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 187433.29

Authors

Xiong, J.-P.,Stehle, T.,Zhang, R.,Joachimiak, A.,Frech, M.,Goodman, S.L.,Arnaout, M.A. (deposition date: 2002-03-06, release date: 2002-04-17, Last modification date: 2023-08-16)

Primary citation

Xiong, J.P.,Stehle, T.,Zhang, R.,Joachimiak, A.,Frech, M.,Goodman, S.L.,Arnaout, M.A.
Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand.
Science, 296:151-155, 2002

PubMed Abstract: The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3.

PubMed: 11884718
DOI: 10.1126/science.1069040

Experimental method

X-RAY DIFFRACTION (3.2 Å)