1MK7
CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN CHIMERA
Summary for 1MK7
Entry DOI | 10.2210/pdb1mk7/pdb |
Related | 1MIX 1MIZ 1MK9 |
Descriptor | Integrin Beta3, TALIN (3 entities in total) |
Functional Keywords | focal adhesion, integrin binding, ferm domain, cytoskeleton, npxy motif, ptb domain, structural protein |
Biological source | Homo sapiens (human) More |
Cellular location | Membrane; Single-pass type I membrane protein: P05106 Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side: P54939 |
Total number of polymer chains | 4 |
Total formula weight | 47831.14 |
Authors | Garcia-Alvarez, B.,De Pereda, J.M.,Calderwood, D.A.,Ulmer, T.S.,Critchley, D.,Campbell, I.D.,Ginsberg, M.H.,Liddington, R.C. (deposition date: 2002-08-28, release date: 2003-01-28, Last modification date: 2024-10-16) |
Primary citation | Garcia-Alvarez, B.,De Pereda, J.M.,Calderwood, D.A.,Ulmer, T.S.,Critchley, D.,Campbell, I.D.,Ginsberg, M.H.,Liddington, R.C. Structural Determinants of Integrin Recognition by Talin Mol.Cell, 11:49-58, 2003 Cited by PubMed Abstract: The binding of cytoplasmic proteins, such as talin, to the cytoplasmic domains of integrin adhesion receptors mediates bidirectional signal transduction. Here we report the crystal structure of the principal integrin binding and activating fragment of talin, alone and in complex with fragments of the beta 3 integrin tail. The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors. In combination with NMR and mutational analysis, our studies reveal the critical interacting elements of both talin and the integrin beta 3 tail, providing structural paradigms for integrin linkage to the cell interior. PubMed: 12535520DOI: 10.1016/S1097-2765(02)00823-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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