1VF6
2.1 Angstrom crystal structure of the PALS-1-L27N and PATJ L27 heterodimer complex
Summary for 1VF6
| Entry DOI | 10.2210/pdb1vf6/pdb |
| Related | 1RSO |
| Descriptor | PALS1-associated tight junction protein, MAGUK p55 subfamily member 5 (3 entities in total) |
| Functional Keywords | l27 domain, heterodimer, four-helical bundle, coiled-coil, hydrophobic packing interactions, protein binding-protein transport complex, protein binding/protein transport |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell junction, tight junction : Q8NI35 Cell membrane; Peripheral membrane protein: Q9JLB2 |
| Total number of polymer chains | 4 |
| Total formula weight | 35564.27 |
| Authors | Li, Y.,Lavie, A.,Margolis, B.,Karnak, D. (deposition date: 2004-04-09, release date: 2004-04-20, Last modification date: 2023-12-27) |
| Primary citation | Li, Y.,Karnak, D.,Demeler, B.,Margolis, B.,Lavie, A. Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes. Embo J., 23:2723-2733, 2004 Cited by PubMed Abstract: L27 is a protein-binding domain that can assemble essential proteins for signaling and cell polarity into complexes by interacting in a heterodimeric manner. One of these protein complexes is the PATJ/PALS1/Crumbs tripartite complex, which is crucial for the establishment and maintenance of cell polarity. To reveal the structural basis underlining the obligate heterodimerization, we have determined the crystal structure of the PALS1-L27N/PATJ-L27 heterodimer complex. Each L27 domain is composed of three helices. The two L27 domains heterodimerize by building a compact structure consisting of a four-helix bundle formed by the first two helices of each L27 domain and one coiled-coil formed by the third helix of each domain. The large hydrophobic packing interactions contributed by all the helices of both L27 domains predominantly drive the heterodimer formation, which is likely to be a general feature of L27 domains. Combined with mutational studies, we can begin to understand the structural basis for the specificity of L27 binding pairs. Our results provide unique insights into L27 domain heterodimer complex, which is critical for cell polarization. PubMed: 15241471DOI: 10.1038/sj.emboj.7600294 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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