2p0c
From Proteopedia
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{{STRUCTURE_2p0c| PDB=2p0c | SCENE= }} | {{STRUCTURE_2p0c| PDB=2p0c | SCENE= }} | ||
- | + | ===Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER=== | |
- | |||
- | ==Overview== | ||
- | A human B-lymphoblastoid lambda gt11 expression library was screened using anti-phosphotyrosine antibodies yielding complementary DNAs encoding active tyrosine kinases. The resulting clones were used to obtain the sequence of a novel 984 amino acid transmembrane tyrosine kinase. Analysis of the complementary DNA revealed extracellular immunoglobulin and fibronectin type III domains and the unusual kinase signature sequence KWIAIES; all are characteristic of the axl family of tyrosine kinases. The novel tyrosine kinase was not expressed in normal B- and T-lymphocytes but, unlike axl, was expressed in numerous neoplastic B- and T-cell lines. Transcripts for the novel receptor-like tyrosine kinase were detected in normal peripheral blood monocytes and bone marrow. One alternatively spliced transcript was detected which contained an insert in the membrane proximal region that could encode for a truncated, soluble receptor. Sequence comparison shows that the kinase may be the human protooncogene for the recently isolated chicken retroviral oncogene v-ryk (recently renamed v-eyk), a truncated tyrosine kinase whose expression by retroviral infection produced sarcomas in chickens. The intracellular domain of the human kinase shows 83% similarity and 71% identity to v-ryk. Since the ryk designation has been used to name another tyrosine kinase and an analysis of RNA expression demonstrated that this novel human kinase is expressed in monocytes and tissues of epithelial and reproductive origin, we have designated our novel protooncogene c-mer. | ||
==About this Structure== | ==About this Structure== | ||
- | 2P0C is a | + | 2P0C is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P0C OCA]. |
==Reference== | ==Reference== | ||
- | + | <ref group="xtra">PMID:8086340</ref><ref group="xtra">PMID:11062461</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
- | [[Category: Single protein]] | ||
[[Category: Arrowsmith, C H.]] | [[Category: Arrowsmith, C H.]] | ||
[[Category: Bochkarev, A.]] | [[Category: Bochkarev, A.]] | ||
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[[Category: Tyrosine-protein kinase]] | [[Category: Tyrosine-protein kinase]] | ||
[[Category: Vision]] | [[Category: Vision]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:12:59 2009'' |
Revision as of 07:13, 18 February 2009
Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER
About this Structure
2P0C is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Graham DK, Dawson TL, Mullaney DL, Snodgrass HR, Earp HS. Cloning and mRNA expression analysis of a novel human protooncogene, c-mer. Cell Growth Differ. 1994 Jun;5(6):647-57. PMID:8086340
- Gal A, Li Y, Thompson DA, Weir J, Orth U, Jacobson SG, Apfelstedt-Sylla E, Vollrath D. Mutations in MERTK, the human orthologue of the RCS rat retinal dystrophy gene, cause retinitis pigmentosa. Nat Genet. 2000 Nov;26(3):270-1. PMID:11062461 doi:10.1038/81555
Page seeded by OCA on Wed Feb 18 09:12:59 2009
Categories: Homo sapiens | Receptor protein-tyrosine kinase | Arrowsmith, C H. | Bochkarev, A. | Dhe-Paganon, S. | Edwards, A M. | Huang, X. | Jr., P J.Finerty. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Walker, J R. | Weigelt, J. | Atp-binding | Disease mutation | Glycoprotein | Kinase | Nucleotide-binding | Phosphorylation | Proto-oncogene | Receptor | Retinitis pigmentosa | Sensory transduction | Sgc | Signal | Structural genomic | Structural genomics consortium | Transferase | Tyrosine-protein kinase | Vision