SOLUTION NMR STRUCTURE OF AGRP(87-120; C105A)
Design, pharmacology, and NMR structure of a minimized cystine knot with agouti-related protein activity.
High Resolution NMR Structure of the Chemically-Synthesized Melanocortin Receptor Binding Domain of Agrp(87-132) of the Agouti-Related Protein.
THIS IS A RATIONALLY MINIMIZED FRAGMENT OF THE FULLY ACTIVE C-TERMINAL DOMAIN OF THE HUMAN AGOUTI-RELATED PROTEIN AGRP(87-132). THIS FRAGMENT HAS REMOVED FROM IT THE LARGELY DISORDERED C-TERMINAL 12 RESIDUES, YET RETAINS THE SAME BASIC STRUCTURAL AND FUNCTIONAL CHARACTERISTICS OF THE LARGER FRAGMENT.
AGRP(87-120:C105A) Non-superimposed structures, same structure family
THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN HOMO SAPIENS. THE SYNTHETIC METHOD IS STANDARD SOLID-PHASE SYNTHESIS FOLLOWED BY AQUEOUS OXIDATIVE FOLDING.
THE NOESY, TOCSY AND DQF-COSY EXPERIMENTS WERE PERFORMED AT 800 MHZ; THE HX STUDY WAS CONDUCTED AT 500 MHZ.
STRUCTURE CALCULATIONS WERE ASSISTED WITH AUTOMATED ASSIGNMENT. FINAL STRUCTURES WERE CALCULATED USING 602 NOE-BASED UPPER LIMIT RESTRAINTS AND 23 ALPHA-TO- AMIDE 3-BOND J-COUPLING CONSTANTS.
1.7 MM AGRP(87-120 NATURAL ABUNDANCE OF ALL NUCLEI.
1.6 MM AGRP(87-120; C105A), NATURAL ABUNDANCE OF ALL NUCLEI.
Krish Krishamurthy, Evan Williams, Steve Cheathum, Frtis Vosman, Dan Iverson, Michael Carlisle, Dan Steele, James Welch
Department of Chemistry,Carlsberg Laboratory, Copenhagen, Denmark
Guntert, P., Mumenthaler, C., and Wuthrich, K.
Bartels, C., Xia, T. H., Billeter, M., Guntert, P., and Wuthrich, K.
RATIONAL PROTEIN DESIGN, ICK, INHIBITOR CYSTINE KNOT, AGRP, AGOUTI-RELATED PROTEIN, MELANOCORTIN, SIGNALING PROTEIN