Search PubMed⌕ Search

Biomedical subjects

Dimitar B Nikolov

Publications and source records attributed to Dimitar B Nikolov.

20 records · Page 2Linked to original sources

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

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 A and has unit-cell parameters a = 128, b = 88, c = 79 A, beta = 112 degrees. The other crystal form grows in space group P1, has unit-cell parameters a = 78, b = 78, c = 78 A, alpha = 69, beta = 75, gamma = 69 degrees and diffracts to 2.7A. 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.

Animals↗

Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding.

GABARAP recognizes and binds the gamma2 subunit of the GABA(A) receptor, interacts with microtubules and the N-ethyl maleimide sensitive factor, and is proposed to function in GABA(A) receptor trafficking and postsynaptic localization. We have determined the crystal structure of human GABARAP at 1.6 A resolution. The structure comprises an N-terminal helical subdomain and a ubiquitin-like C-terminal domain. Structure-based mutational analysis demonstrates that the N-terminal subdomain is responsible for tubulin binding while the C-terminal domain contains the binding site for the GABA(A). A second GABARAP crystal form was determined at 1.9 A resolution and documents that GABARAP can self-associate in a head-to-tail manner. The structural details of this oligomerization reveal how GABARAP can both promote tubulin polymerization and facilitate GABA(A) receptor clustering.

Adaptor Proteins, Signal Transducing↗