1LKY
Structure of the wild-type TEL-SAM polymer
Summary for 1LKY
| Entry DOI | 10.2210/pdb1lky/pdb |
| Descriptor | TRANSCRIPTION FACTOR ETV6, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | leukemia, tyrosine kinase, transcriptional repression, drug design, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P41212 P41212 |
| Total number of polymer chains | 6 |
| Total formula weight | 56698.08 |
| Authors | Tran, H.H.,Kim, C.A.,Faham, S.,Bowie, J.U. (deposition date: 2002-04-26, release date: 2002-06-12, Last modification date: 2023-08-16) |
| Primary citation | Tran, H.H.,Kim, C.A. Native interface of the SAM domain polymer of TEL. BMC STRUCT.BIOL., 2:5-5, 2002 Cited by PubMed Abstract: TEL is a transcriptional repressor containing a SAM domain that forms a helical polymer. In a number of hematologic malignancies, chromosomal translocations lead to aberrant fusions of TEL-SAM to a variety of other proteins, including many tyrosine kinases. TEL-SAM polymerization results in constitutive activation of the tyrosine kinase domains to which it becomes fused, leading to cell transformation. Thus, inhibitors of TEL-SAM self-association could abrogate transformation in these cells. In previous work, we determined the structure of a mutant TEL-SAM polymer bearing a Val to Glu substitution in center of the subunit interface. It remained unclear how much the mutation affected the architecture of the polymer, however. PubMed: 12193272DOI: 10.1186/1472-6807-2-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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