1YUK

The crystal structure of the PSI/Hybrid domain/ I-EGF1 segment from the human integrin beta2 at 1.8 resolution

Summary for 1YUK

• Entry DOI: 10.2210/pdb1yuk/pdb
• Descriptor: Integrin beta-2 A chain, Integrin beta-2 B chain, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: integrin beta2, hybrid domain, psi domain, i-egf domain, crystal structure of psi/hybrid/i-egf1, cell adhesion
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P05107 P05107
• Total number of polymer chains: 2
• Total formula weight: 25312.55

Authors

Shi, M.,Sundramurthy, K.,Liu, B.,Tan, S.M.,Law, S.K.,Lescar, J. (deposition date: 2005-02-14, release date: 2005-07-19, Last modification date: 2024-11-13)

Primary citation

Shi, M.,Sundramurthy, K.,Liu, B.,Tan, S.M.,Law, S.K.,Lescar, J.
The Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin {beta}2 Subunit at 1.8-A Resolution
J.Biol.Chem., 280:30586-30593, 2005

PubMed Abstract: Integrins are modular (alphabeta) heterodimeric proteins that mediate cell adhesion and convey signals across the plasma membrane. Interdomain motions play a key role in signal transduction by propagating structural changes through the molecule, thus controlling the activation state and adhesive properties of the integrin. We expressed a soluble fragment of the human integrin beta2 subunit comprising the plexin-semaphorin-integrin domain (PSI)/hybrid domain/I-EGF1 fragment and present its crystal structure at 1.8-A resolution. The structure reveals an elongated molecule with a rigid architecture stabilized by nine disulfide bridges. The PSI domain is located centrally and participates in the formation of extended interfaces with the hybrid domain and I-EGF1 domains, respectively. The hybrid domain/PSI interface involves the burial of an Arg residue, and contacts between PSI and I-EGF1 are mainly mediated by well conserved Arg and Trp residues. Conservation of key interacting residues across the various integrin beta subunits sequences suggests that our structure represents a good model for the entire integrin family. Superposition with the integrin beta3 receptor in its bent conformation suggests that an articulation point is present at the linkage between its I-EGF1 and I-EGF2 modules and underlines the importance of this region for the control of integrin-mediated cell adhesion.

PubMed: 15965234
DOI: 10.1074/jbc.M502525200

Experimental method

X-RAY DIFFRACTION (1.8 Å)