2EMT
Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1
Summary for 2EMT
| Entry DOI | 10.2210/pdb2emt/pdb |
| Related | 1GC6 1GC7 1J19 2D10 2D11 2D2Q 2EMS |
| Descriptor | Radixin, P-selectin glycoprotein ligand 1 (2 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 Cell membrane ; Single-pass membrane protein : Q62170 |
| Total number of polymer chains | 5 |
| Total formula weight | 82633.00 |
| Authors | Takai, Y.,Kitano, K.,Terawaki, S.,Maesaki, R.,Hakoshima, T. (deposition date: 2007-03-28, release date: 2008-03-18, Last modification date: 2023-10-25) |
| Primary citation | Takai, Y.,Kitano, K.,Terawaki, S.,Maesaki, R.,Hakoshima, T. Structural basis of PSGL-1 binding to ERM proteins Genes Cells, 12:1329-1338, 2007 Cited by PubMed Abstract: P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory responses. On activation, ezrin-radixin-moesin (ERM) proteins mediate the redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to target molecules. ERM proteins recognize a short binding motif, Motif-1, conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks Motif-1 residues important for binding to ERM proteins. The crystal structure of the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide reveals that the peptide binds the groove of FERM subdomain C by forming a beta-strand associated with strand beta5C, followed by a loop flipped out towards the solvent. The Motif-1 3(10) helix present in the FERM-ICAM-2 complex is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are occupied by large residues Met9 and His8, which stabilize peptide conformation and enhance groove binding. Non-conserved residues play an important role in compensating for loss of binding energy resulting from the absence of conserved residues important for binding. PubMed: 18076570DOI: 10.1111/j.1365-2443.2007.01137.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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