Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.10.1 extracted from

  • Bocharov, E.V.; Mayzel, M.L.; Volynsky, P.E.; Goncharuk, M.V.; Ermolyuk, Y.S.; Schulga, A.A.; Artemenko, E.O.; Efremov, R.G.; Arseniev, A.S.
    Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 (2008), J. Biol. Chem., 283, 29385-29395.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information local environment and membrane surface potential can modulate dimerization and activation of the receptor Homo sapiens

Application

Application Comment Organism
additional information possible physiological role of the EphA1 receptor as an extracellular pH sensor. Glu547 may serve as a sensor of the environment surrounding the EphA1 receptor on the cell surface, and its deprotonation may partly disrupt the coupling between the extracellular and cytoplasmic domains of the receptor because of transient local melting of helical structure and thus modulate signal transduction Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
38-residue EphA1 fragment 536–573 expressed in Escherichia coli BL21(DE3)pLysS Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Homo sapiens 5737
-
membrane EphA1 transmembrane segments associate in a right-handed parallel alpha-helical bundle, region (544-569)2, through the N-terminal glycine zipper motif A550X3G554X3G558. Dimerization of the transmembrane fragment of the EphA1 receptor Homo sapiens 16020
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by gel filtration Homo sapiens

Subunits

Subunits Comment Organism
homodimer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
EphA1
-
Homo sapiens
EphA1 receptor
-
Homo sapiens
receptor tyrosine kinase EphA1
-
Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
4.3 6.3 under acidic conditions, the N terminus of the transmembrane helix is stabilized by an N-capping box formed by the uncharged carboxyl group of Glu547, whereas its deprotonation results in a rearrangement of hydrogen bonds, fractional unfolding of the helix, and a realignment of the helix-helix packing with appearance of additional minor dimer conformation utilizing seemingly the C-terminal GG4-like dimerization motif A560X3G564 Homo sapiens