Receptor kinaznog umetnutog domena
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| Receptor kinaznog umetnutog domena (tip III receptorske tirozinske kinaze) | |||||||||||
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 Prikaz bazirna na 1VR2 | |||||||||||
| Dostupne strukture | |||||||||||
| 1VR2, 1Y6A, 1Y6B, 1YWN, 2M59, 2OH4, 2P2H, 2P2I, 2QU5, 2QU6, 2RL5, 2X1W, 2X1X, 2XIR, 3B8Q, 3B8R, 3BE2, 3C7Q, 3CJF, 3CJG, 3CP9, 3CPB, 3CPC, 3DTW, 3EFL, 3EWH, 3KVQ, 3S35, 3S36, 3S37, 3U6J, 3V2A, 3V6B, 3VHE, 3VHK, 3VID, 3VNT, 3VO3, 4AG8, 4AGC, 4AGD, 4ASD, 4ASE | |||||||||||
| Identifikatori | |||||||||||
| Simboli | KDR; CD309; FLK1; VEGFR; VEGFR2 | ||||||||||
| Vanjski ID | OMIM: 191306 MGI: 96683 HomoloGene: 55639 GeneCards: KDR Gene | ||||||||||
| EC broj | 2.7.10.1 | ||||||||||
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| Pregled RNK izražavanja | |||||||||||
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| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 3791 | 16542 | |||||||||
| Ensembl | ENSG00000128052 | ENSMUSG00000062960 | |||||||||
| UniProt | P35968 | Q8VCD0 | |||||||||
| Ref. Sekv. (iRNK) | NM_002253 | NM_010612 | |||||||||
| Ref. Sekv. (protein) | NP_002244 | NP_034742 | |||||||||
| Lokacija (UCSC) | Chr 4: 55.94 - 55.99 Mb | Chr 5: 75.93 - 75.98 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
Receptor kinaznog umetnutog domena (KDR, tip III receptorske tirozinske kinaze, receptor 2 vakkularnog endotelnog faktora rasta, VEGFR-2, Flk1, fetalna jetrena kinaza 1) je VEGF receptor. KDR je ljudski gen koji kodira ovaj enzim. KDR se takođe označava sa CD309 (klaster diferencijacije 309).
Interakcije
Receptor kinaznog umetnutog domena formira interakcije sa SHC2,[1] Aneksin A5[2] i SHC1.[3][4]
Vidi još
- Klaster diferencijacije
- VEGF receptori
Reference
- ↑ Warner, A J; Lopez-Dee J; Knight E L; Feramisco J R; Prigent S A (April 2000). „The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells”. Biochem. J. (England) 347 (Pt 2): 501–9. DOI:10.1042/0264-6021:3470501. ISSN 0264-6021. PMC 1220983. PMID 10749680.
- ↑ Wen, Y; Edelman J L; Kang T; Sachs G (May 1999). „Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1”. Biochem. Biophys. Res. Commun. (UNITED STATES) 258 (3): 713–21. DOI:10.1006/bbrc.1999.0678. ISSN 0006-291X. PMID 10329451.
- ↑ Zanetti, Adriana; Lampugnani Maria Grazia; Balconi Giovanna; Breviario Ferruccio; Corada Monica; Lanfrancone Luisa; Dejana Elisabetta (April 2002). „Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling”. Arterioscler. Thromb. Vasc. Biol. (United States) 22 (4): 617–22. DOI:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700.
- ↑ D'Angelo, G; Martini J F; Iiri T; Fantl W J; Martial J; Weiner R I (May 1999). „16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells”. Mol. Endocrinol. (UNITED STATES) 13 (5): 692–704. DOI:10.1210/me.13.5.692. ISSN 0888-8809. PMID 10319320.
Literatura
- Holmes K, Roberts OL, Thomas AM, Cross MJ. (October 2007). „Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition.”. Cell Signal. 19 (10): 2003–2012. DOI:10.1016/j.cellsig.2007.05.013. PMID 17658244.
- Petrova TV, Makinen T, Alitalo K (1999). „Signaling via vascular endothelial growth factor receptors.”. Exp. Cell Res. 253 (1): 117–30. DOI:10.1006/excr.1999.4707. PMID 10579917.
- Sato Y, Kanno S, Oda N, et al. (2000). „Properties of two VEGF receptors, Flt-1 and KDR, in signal transduction.”. Ann. N. Y. Acad. Sci. 902 (1): 201–5; discussion 205–7. DOI:10.1111/j.1749-6632.2000.tb06314.x. PMID 10865839.
- Zachary I, Gliki G (2001). „Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family.”. Cardiovasc. Res. 49 (3): 568–81. DOI:10.1016/S0008-6363(00)00268-6. PMID 11166270.
- Vené R, Benelli R, Noonan DM, Albini A (2001). „HIV-Tat dependent chemotaxis and invasion, key aspects of tat mediated pathogenesis.”. Clin. Exp. Metastasis 18 (7): 533–8. DOI:10.1023/A:1011991906685. PMID 11688957.
- Lenton K (2003). „VEGFR-2 (KDR/Flk-1).”. J. Biol. Regul. Homeost. Agents 16 (3): 227–32. PMID 12456025.
- Matsumoto T, Mugishima H (2006). „Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis.”. J. Atheroscler. Thromb. 13 (3): 130–5. DOI:10.5551/jat.13.130. PMID 16835467.
Vanjske veze
- MeSH Kinase+insert+domain+receptor
- p
- r
- u
PDB Galerija
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