The Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor (RLF)

Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor.

residue 132 is a glycine linked through the C-terminal carboxyl group to the 6-amino group of lysine 50 of the RLF B chain

residue 50 is a lysine linked through the 6-amino group to the C-terminal carboxyl group of glycine132

Solution Structure Of The Relaxin-Like Factor

Leydig insulin-like hormone [Homo sapiens]

Similar to insulin-like 3 (Leydig cell), partial [Homo sapiens]

Insulin-like 3 (Leydig cell) [Homo sapiens]

tyrosine-protein kinase JAK3 precursor [Pan troglodytes]

insulin-like 3 isoform 2 precursor [Homo sapiens]

PREDICTED: insulin-like 3 isoform X2 [Nomascus leucogenys]

PREDICTED: insulin-like 3 [Papio anubis]

PREDICTED: insulin-like 3 [Chlorocebus sabaeus]

RecName: Full=Insulin-like 3; AltName: Full=Leydig insulin-like peptide; Short=Ley-I-L; AltName: Full=Relaxin-like factor; Cont

A chain of human RLF C-terminally extended by Gly cross-linked through the C-terminus to the 6-amino group of Lys(50)

B chain of human RLF cross-linked through the 6-amino group of Lys(B50) to the carboxyl group of Gly(132) at the terminus of the A chain

torsion angle dynamics, simulated annealing

cross-linked derivative determine under the same experimental conditions

Ambiguous restraints for interactive assignment

Predicting protein torsion angle restraints

Institute Pasteur
Unit de Bioinformatique
Structurale
25-28 rue du Dr Roux
F-75724 Paris CEDEX 15

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax

Department of Biochemistry
University of Alberta, Edmonton, Canada

Brunger, Adams, Clore, Gros, Nilges and Read