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2gsf
From Proteopedia
| 2gsf, resolution 1.77Å () | |||||||||
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| Gene: | EPHA3, ETK, ETK1, HEK (Homo sapiens) | ||||||||
| Activity: | Receptor protein-tyrosine kinase, with EC number 2.7.10.1 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
The Human Epha3 Receptor Tyrosine Kinase and Juxtamembrane Region
Disease
[EPHA3_HUMAN] Defects in EPHA3 may be a cause of colorectal cancer (CRC) [MIM:114500].
Function
[EPHA3_HUMAN] Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.[1]
About this Structure
2gsf is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- ↑ Lawrenson ID, Wimmer-Kleikamp SH, Lock P, Schoenwaelder SM, Down M, Boyd AW, Alewood PF, Lackmann M. Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling. J Cell Sci. 2002 Mar 1;115(Pt 5):1059-72. PMID:11870224
Categories: Homo sapiens | Receptor protein-tyrosine kinase | Arrowsmith, C H. | Bochkarev, A. | Davis, T. | Dhe-Paganon, S. | Dong, A. | Edwards, A M. | MacKenzie, F. | Newman, E M. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Walker, J R. | Weigelt, J. | Atp-binding | Kinase | Membrane | Nucleotide-binding | Phosphorylation | Receptor | Sgc | Structural genomic | Structural genomics consortium | Transferase | Transmembrane | Tyrosine-protein kinase

