1Q68
Solution structure of T-cell surface glycoprotein CD4 and Proto-oncogene tyrosine-protein kinase LCK fragments
Summary for 1Q68
| Entry DOI | 10.2210/pdb1q68/pdb |
| NMR Information | BMRB: 5944 |
| Descriptor | T-cell surface glycoprotein CD4, Proto-oncogene tyrosine-protein kinase LCK, ZINC ION (3 entities in total) |
| Functional Keywords | peptide-peptide complex, helix-helix interaction, zinc coordination, beta hairpin, membrane protein-transferase complex, membrane protein/transferase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P01730 Cytoplasm: P06239 |
| Total number of polymer chains | 2 |
| Total formula weight | 8058.59 |
| Authors | Kim, P.W.,Sun, Z.Y.,Blacklow, S.C.,Wagner, G.,Eck, M.J. (deposition date: 2003-08-12, release date: 2003-11-25, Last modification date: 2024-05-22) |
| Primary citation | Kim, P.W.,Sun, Z.Y.,Blacklow, S.C.,Wagner, G.,Eck, M.J. A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science, 301:1725-1728, 2003 Cited by PubMed Abstract: The T cell coreceptors CD4 and CD8 both associate via their cytoplasmic tails with the N-terminus of the Src-family tyrosine kinase Lck. These interactions require zinc and are critical for T cell development and activation. We examined the folding and solution structures of ternary CD4-Lck-Zn2+ and CD8alpha-Lck-Zn2+ complexes. The coreceptor tails and the Lck N-terminus are unstructured in isolation but assemble in the presence of zinc to form compactly folded heterodimeric domains. The cofolded complexes have similar "zinc clasp" cores that are augmented by distinct structural elements. A dileucine motif required for clathrin-mediated endocytosis of CD4 is masked by Lck. PubMed: 14500983DOI: 10.1126/science.1085643 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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