1JI7

Crystal Structure of TEL SAM Polymer

Summary for 1JI7

• Entry DOI: 10.2210/pdb1ji7/pdb
• Related: 1BQV
• Descriptor: ETS-RELATED PROTEIN TEL1, SULFATE ION (3 entities in total)
• Functional Keywords: helical polymer, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P41212
• Total number of polymer chains: 3
• Total formula weight: 33327.74

Authors

Kim, C.A.,Phillips, M.L.,Kim, W.,Gingery, M.,Tran, H.H.,Robinson, M.A.,Faham, S.,Bowie, J.U. (deposition date: 2001-06-29, release date: 2002-07-03, Last modification date: 2024-11-20)

Primary citation

Kim, C.A.,Phillips, M.L.,Kim, W.,Gingery, M.,Tran, H.H.,Robinson, M.A.,Faham, S.,Bowie, J.U.
Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression.
EMBO J., 20:4173-4182, 2001

PubMed Abstract: TEL is a transcriptional repressor that is a frequent target of chromosomal translocations in a large number of hematalogical malignancies. These rearrangements fuse a potent oligomerization module, the SAM domain of TEL, to a variety of tyrosine kinases or transcriptional regulatory proteins. The self-associating property of TEL-SAM is essential for cell transformation in many, if not all of these diseases. Here we show that the TEL-SAM domain forms a helical, head-to-tail polymeric structure held together by strong intermolecular contacts, providing the first clear demonstration that SAM domains can polymerize. Our results also suggest a mechanism by which SAM domains could mediate the spreading of transcriptional repression complexes along the chromosome.

PubMed: 11483520
DOI: 10.1093/emboj/20.15.4173

Experimental method

X-RAY DIFFRACTION (1.45 Å)