1J19
Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide
Summary for 1J19
| Entry DOI | 10.2210/pdb1j19/pdb |
| Related | 1E5W 1EF1 1GC6 1GC7 1ISN |
| Descriptor | radixin, 16-mer peptide from Intercellular adhesion molecule-2 (3 entities in total) |
| Functional Keywords | protein-peptide complex, cell adhesion |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043 Membrane; Single-pass type I membrane protein: P35330 |
| Total number of polymer chains | 2 |
| Total formula weight | 39305.29 |
| Authors | Hamada, K.,Shimizu, T.,Yonemura, S.,Tsukita, S.,Tsukita, S.,Hakoshima, T. (deposition date: 2002-12-02, release date: 2003-03-11, Last modification date: 2023-10-25) |
| Primary citation | Hamada, K.,Shimizu, T.,Yonemura, S.,Tsukita, S.,Tsukita, S.,Hakoshima, T. Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex EMBO J., 22:502-514, 2003 Cited by PubMed Abstract: ERM (ezrin/radixin/moesin) proteins recognize the cytoplasmic domains of adhesion molecules in the formation of the membrane-associated cytoskeleton. Here we report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the ICAM-2 cytoplasmic peptide. The non-polar region of the ICAM-2 peptide contains the RxxTYxVxxA sequence motif to form a beta-strand followed by a short 3(10)-helix. It binds the groove of the phosphotyrosine-binding (PTB)-like subdomain C mediated by a beta-beta association and several side-chain interactions. The binding mode of the ICAM-2 peptide to the FERM domain is distinct from that of the NPxY motif-containing peptide binding to the canonical PTB domain. Mutation analyses based on the crystal structure reveal the determinant elements of recognition and provide the first insights into the physical link between adhesion molecules and ERM proteins. PubMed: 12554651DOI: 10.1093/emboj/cdg039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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