2p0c
From Proteopedia
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|PDB= 2p0c |SIZE=350|CAPTION= <scene name='initialview01'>2p0c</scene>, resolution 2.40Å | |PDB= 2p0c |SIZE=350|CAPTION= <scene name='initialview01'>2p0c</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span> |
|GENE= MERTK, MER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= MERTK, MER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0c OCA], [http://www.ebi.ac.uk/pdbsum/2p0c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p0c RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
- | |||
- | ==Disease== | ||
- | Known diseases associated with this structure: Blood group, Raph OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602243 602243]], Nephropathy with pretibial epidermolysis bullosa and deafness OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602243 602243]], Retinitis pigmentosa-38 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604705 604705]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Walker, J R.]] | [[Category: Walker, J R.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
- | [[Category: ANP]] | ||
- | [[Category: BME]] | ||
- | [[Category: MG]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: disease mutation]] | [[Category: disease mutation]] | ||
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[[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 Mon Mar 31 04:26:08 2008'' |
Revision as of 01:26, 31 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | , , | ||||||
Gene: | MERTK, MER (Homo sapiens) | ||||||
Activity: | Receptor protein-tyrosine kinase, with EC number 2.7.10.1 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
2P0C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Cloning and mRNA expression analysis of a novel human protooncogene, c-mer., Graham DK, Dawson TL, Mullaney DL, Snodgrass HR, Earp HS, Cell Growth Differ. 1994 Jun;5(6):647-57. PMID:8086340
Page seeded by OCA on Mon Mar 31 04:26:08 2008
Categories: Homo sapiens | Receptor protein-tyrosine kinase | Single protein | 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