Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex Journal Article


Authors: Himanen, J. P.; Nikolov, D. B.
Article Title: Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex
Abstract: Eph receptors and their ephrin ligands are involved in various aspects of cell-cell communication during development, including those of the axon pathfinding processes in the nervous system and cell-cell interactions of the vascular endothelial cells. The recognition and binding properties of the ligand-binding domain of EphB2 receptor and the extracellular domain of ephrin-B2 have been studied and two different cocrystals of their complex have been generated. One crystal form has space group C2, diffracts to 3.5 Å and has unit-cell parameters a = 128, b = 88, c = 79 Å, β = 112°. The other crystal form grows in space group P1, has unit-cell parameters a = 78, b = 78, c = 78 Å, α = 69, β = 75, γ = 69° and diffracts to 2.7 Å. Structure-determination experiments using the latter form are in progress. The structure of the complex will elucidate the chemical nature of the interactions between Eph receptors and ephrins, which would create the possibility of using them as targets for structure-based anticancer-drug development.
Keywords: genetics; protein conformation; mouse; animal; animals; mice; membrane proteins; protein tyrosine kinase; chemistry; recombinant proteins; membrane protein; recombinant protein; receptor protein-tyrosine kinases; crystallization; ephrin receptor b2; receptor, ephb2; ephrin b2; ephrin-b2; article
Journal Title: Acta Crystallographica Section D: Biological Crystallography
Volume: D58
Issue: Pt 3
ISSN: 0907-4449
Publisher: Wiley Blackwell  
Date Published: 2002-03-01
Start Page: 533
End Page: 535
Language: English
DOI: 10.1107/s0907444902000264
PUBMED: 11856847
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 14 November 2014 -- Source: Scopus
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  1. Dimitar B Nikolov
    86 Nikolov
  2. Juha P Himanen
    50 Himanen