MONOCLINIC FORM OF HUMAN TRANSTHYRETIN COMPLEXED WITH THYROXINE (T4)

Structure of a new polymorphic monoclinic form of human transthyretin at 3 A resolution reveals a mixed complex between unliganded and T4-bound tetramers of TTR.

STRUCTURAL ASPECTS OF INOTROPIC BIPYRIDINE BINDING. CRYSTAL STRUCTURE DETERMINATION TO 1.9 A OF THE HUMAN SERUM TRANSTHYRETIN-MILRINONE COMPLEX

MECHANISM OF MOLECULAR RECOGNITION. STRUCTURAL ASPECTS OF 3,3'-DIIODO-L-THYRONINE BINDING TO HUMAN SERUM TRANSTHYRETIN

STRUCTURES OF HUMAN TRANSTHYRETIN COMPLEXED WITH THYROXINE AT 2.0 A RESOLUTION AND 3',5'-DINITRO-N-ACETYL-L-THYRONINE AT 2.2 A RESOLUTION

HANGMAN HANGING DROP CRYSTALLIZATION METHOD
55% AMMONIUM SULFATE; 0.1 M PHOSPHATE BUFFER, pH 4.9, HANGMAN HANGING DROP CRYSTALLIZATION METHOD, temperature 293K

TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH THYROXINE (T4)

THIS COORDINATE SET COMPRISES TWO DEFFERENT HUMAN TTR TETRAMERS
AN APO ONE (CHAINS E-H) AND A T4-BOUND ONE (CHAINS A-D).
THERE ARE NO WATER MOLECULES INCLUDED IN THE MODEL.
RESIDUES 1-9 AND 126-127 OF ALL A-H CHAINS ARE ILL-DEFINED IN THE ELECTRON DENSITY
MAPS AND HAVE BEEN OMITTED.

GROUPED B FACTOR HAVE BEEN REFINED
(FOR MAIN AND SIDRCHAIN ATOMS)
B RMSD FOR BONDED MAINCHAIN ATOMS = 8.628
B RMSD FOR BONDED SIDECHAIN ATOMS = 11.213
B RMSD FOR ANGLE MAINCHAIN ATOMS = 13.280
B RMSD FOR ANGLE SIDECHAIN ATOMS == 16.102

NCS RESTRAINTS. DETAILS INFORMATIONS:
MAIN CHAIN ATOMS SELECTED
EFFECTIVE FORCE CONSTANT FOR NCS POSITIONAL RESTRAINTS
= 10.00 Kcal/mol-A**2
TARGET DEVIATION OF NCS RELATED B FACTORS FROM AVERAGE
= 2.500 A**2
SIDE CHAIN ATOMS SELECTED
EFFECTIVE FORCE CONSTANT FOR NCS POSITIONAL RESTRAINTS
= 5.00 Kcal/mol-A**2
TARGET DEVIATION OF NCS RELATED B FACTORS FROM AVERAGE
= 2.00 A**2

TETRAMER GENERATED FROM PDB ENTRY 2ROX WITH ONLY PROTEIN ATOMS FROM RESIDUES 10-125 INCLUDED

ALBUMIN, TRANSPORT, AMYLOID, THYROID HORMONE, LIVER, PLASMA, POLYNEUROPATHY, THYROXINE, PREALBUMIN, GREEK KEY BETA BARREL, TRANSPORT PROTEIN