Crystal structure of the human alpha1B adrenergic receptor in complex with inverse agonist (+)-cyclazosin

Crystal structure of the alpha 1B -adrenergic receptor reveals molecular determinants of selective ligand recognition.

Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.,Residues 38-350 represent the human alpha1B adrenergic receptor, mutant B1 (alpha1B-AR-B1). Residues 249 to 283 were deleted for crystallisation purposes. Residues 351 to 359 form a linker connecting alpha1B-AR-B1 with the DARPin crystallisation chaperone. Residues 360 to 515 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 516 to 518 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 519 to 524 are part of the HRV 3C protease recognition sequence visible in the electron density.
Alpha-1B adrenergic receptor,alpha1B adrenergic receptor,Alpha-1B adrenergic receptor,alpha1B adrenergic receptor,Alpha-1B adrenergic receptor,alpha1B adrenergic receptor,Alpha-1B adrenergic receptor,alpha1B adrenergic receptor

GPGSSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLCFTVLPFSAALEVLGY
WVLGRTFCDIWAAMDVLCCTASILSLCAISIDRYIGVRYYLQYPTLVTRRKAILALLCVWVLSTVISIGPLLVWKEPAPN
YDKVCGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSFKFSREKKAAKMLGIVVGMFIL
CWLPFFIALPLGSLFSTLKPPDAVFKVLLWLGYFNSCLNPIIYLCAEDLVEDWEKARKLLEAARKGQDDEVRILLANGAD
VNTADETGFTPLHLAAWEGHLGIVEVLLKNGADVNANDERGHTPLHLAAYTGHLEIVEVLLKNGAGVNATDVIGTAPLHL
AAMWGHLEIVEVLLKNGADVNAQDKFGKTPFDLAIDNGNEDIAEVLQKAATRELEVLFQ

100 mM MES
400-480 mM Li citrate
28-33% (w/v) PEG400
10 mM L-glutathione reduced form
10 uM cyclazosin

Hydrogens have been added in their riding positions

GPCR-ligand complex, alpha1B adrenergic receptor, cyclazosin, inverse agonist, MEMBRANE PROTEIN