2LQR
NMR structure of Ig3 domain of palladin
Summary for 2LQR
| Entry DOI | 10.2210/pdb2lqr/pdb |
| NMR Information | BMRB: 15512 |
| Descriptor | Palladin (1 entity in total) |
| Functional Keywords | actin binding protein, immunoglubulin, protein binding |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cytoplasm, cytoskeleton: Q9ET54 |
| Total number of polymer chains | 1 |
| Total formula weight | 11991.61 |
| Authors | Beck, M.R.,Dixon IV, R.D.S.,Otey, C.A.,Campbell, S.L.,Murphy, G.S. (deposition date: 2012-03-13, release date: 2013-01-23, Last modification date: 2024-05-01) |
| Primary citation | Beck, M.R.,Dixon, R.D.,Goicoechea, S.M.,Murphy, G.S.,Brungardt, J.G.,Beam, M.T.,Srinath, P.,Patel, J.,Mohiuddin, J.,Otey, C.A.,Campbell, S.L. Structure and Function of Palladin's Actin Binding Domain. J.Mol.Biol., 425:3325-3337, 2013 Cited by PubMed Abstract: Here, we report the NMR structure of the actin-binding domain contained in the cell adhesion protein palladin. Previously, we demonstrated that one of the immunoglobulin domains of palladin (Ig3) is both necessary and sufficient for direct filamentous actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and cross-linking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin cross-linking mechanism that involves concurrent attachment of two actin filaments by a single palladin molecule by an electrostatic mechanism. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo. PubMed: 23806659DOI: 10.1016/j.jmb.2013.06.016 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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