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Ephrin receptor

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== Function ==
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'''Ephrin receptors''' (EPHR) are components of the cell signaling pathways. They belong to the receptor tyrosine kinases. The extracellular ligand-binding domain (LBD) interacts with ephrin<ref>PMID:21078817</ref>. For more details see [[ Ephrin Type-A Receptor]].
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==Relevance ==
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EPHR and ephrins can act as both tumor suppressors and tumor enhancers depending on the context<ref>PMID:20810264</ref>.
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== Structural highlights ==
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EPHR domains include an ectodomain (residues 23-435) containing the LBD (residues 23-326), a second fibronectin III domain (fn3) (residues 446-539), a transmembrane domain (residues 539-563), a kinase domain (residues 596-900) and a sterile-α-motif (SAM) domain (residues 908-972).
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'''Ephrin receptors''' (EPHR) are components of the cell signaling pathways. They belong to the receptor tyrosine kinases. The extracellular ligand-binding domain (LBD) interacts with ephrin. EPHR domains include an ectodomain (residues 23-435) containing the LBD (residues 23-326), a second fibronectin III domain (fn3) (residues 446-539), a transmembrane domain (residues 539-563), a kinase domain (residues 596-900) and a sterile-α-motif (SAM) domain (residues 908-972). For more details see [[ Ephrin Type-A Receptor]].
 
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== References ==
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<references/>

Revision as of 19:31, 19 January 2016

Image:3hei.png
Crystal Structure of ephrin A2 receptor complex with ephrin, 3hei

Template:STRUCTURE 3fxx













Contents

Function

Ephrin receptors (EPHR) are components of the cell signaling pathways. They belong to the receptor tyrosine kinases. The extracellular ligand-binding domain (LBD) interacts with ephrin[1]. For more details see Ephrin Type-A Receptor.

Relevance

EPHR and ephrins can act as both tumor suppressors and tumor enhancers depending on the context[2].

Structural highlights

EPHR domains include an ectodomain (residues 23-435) containing the LBD (residues 23-326), a second fibronectin III domain (fn3) (residues 446-539), a transmembrane domain (residues 539-563), a kinase domain (residues 596-900) and a sterile-α-motif (SAM) domain (residues 908-972).









3D Structures of ephrin receptors

Updated on 19-January-2016


References

  1. ↑ Pitulescu ME, Adams RH. Eph/ephrin molecules--a hub for signaling and endocytosis. Genes Dev. 2010 Nov 15;24(22):2480-92. doi: 10.1101/gad.1973910. PMID:21078817 doi:http://dx.doi.org/10.1101/gad.1973910
  2. ↑ Genander M, Frisen J. Ephrins and Eph receptors in stem cells and cancer. Curr Opin Cell Biol. 2010 Oct;22(5):611-6. doi: 10.1016/j.ceb.2010.08.005. PMID:20810264 doi:http://dx.doi.org/10.1016/j.ceb.2010.08.005

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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