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X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS
Descriptor:	BETA B2-CRYSTALLIN, BETA-MERCAPTOETHANOL
Authors:	Bax, B, Lapatto, R, Nalini, V, Driessen, H, Lindley, P.F, Mahadevan, D, Blundell, T.L, Slingsby, C.
Deposit date:	1992-09-21
Release date:	1993-10-31
Last modified:	2011-07-13
Method:	X-RAY DIFFRACTION (2.1 Å)
Cite:	X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins. Nature, 347, 1990

SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL EXTENDED, NMR, 20 STRUCTURES
Descriptor:	G-PROTEIN COUPLED RECEPTOR KINASE 2
Authors:	Fushman, D, Cowburn, D.
Deposit date:	1997-11-21
Release date:	1998-02-25
Last modified:	2022-02-16
Method:	SOLUTION NMR
Cite:	The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. J.Biol.Chem., 273, 1998

CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS
Descriptor:	BETA B2-CRYSTALLIN
Authors:	Nalini, V, Bax, B, Driessen, H, Moss, D.S, Lindley, P.F, Slingsby, C.
Deposit date:	1993-12-22
Release date:	1994-12-20
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (3.3 Å)
Cite:	Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions. J.Mol.Biol., 236, 1994