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1P5T

Crystal Structure of Dok1 PTB Domain

Summary for 1P5T
Entry DOI10.2210/pdb1p5t/pdb
DescriptorDocking protein 1 (2 entities in total)
Functional Keywordssignaling protein
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm (By similarity): P97465
Total number of polymer chains2
Total formula weight28934.00
Authors
Shi, N.,Ye, S.,Liu, Y.,Zhou, W.,Ding, Y.,Lou, Z.,Qiang, B.,Yuan, J.,Rao, Z. (deposition date: 2003-04-28, release date: 2004-02-17, Last modification date: 2024-10-16)
Primary citationShi, N.,Ye, S.,Bartlam, M.,Yang, M.,Wu, J.,Liu, Y.,Sun, F.,Han, X.,Peng, X.,Qiang, B.,Yuan, J.,Rao, Z.
Structural Basis for the Specific Recognition of RET by the Dok1 Phosphotyrosine Binding Domain
J.BIOL.CHEM., 279:4962-4969, 2004
Cited by
PubMed Abstract: Dok1 is a common substrate of activated protein-tyrosine kinases. It is rapidly tyrosine-phosphorylated in response to receptor tyrosine activation and interacts with ras GTPase-activating protein and Nck, leading to inhibition of ras signaling pathway activation and the c-Jun N-terminal kinase (JNK) and c-Jun activation, respectively. In chronic myelogenous leukemia cells, it has shown constitutive phosphorylation. The N-terminal phosphotyrosine binding (PTB) domain of Dok1 can recognize and bind specifically to phosphotyrosine-containing motifs of receptors. Here we report the crystal structure of the Dok1 PTB domain alone and in complex with a phosphopeptide derived from RET receptor tyrosine kinase. The structure consists of a beta-sandwich composed of two nearly orthogonal, 7-stranded, antiparallel beta-sheets, and it is capped at one side by a C-terminal alpha-helix. The RET phosphopeptide binds to Dok1 via a surface groove formed between strand beta5 and the C-terminal alpha-helix of the PTB domain. The structures reveal the molecular basis for the specific recognition of RET by the Dok1 PTB domain. We also show that Dok1 does not recognize peptide sequences from TrkA and IL-4, which are recognized by Shc and IRS1, respectively.
PubMed: 14607833
DOI: 10.1074/jbc.M311030200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

226707

数据于2024-10-30公开中

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