THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A
Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A.
1QGM belongs to a family of granulin-like repeats
1FWO belongs to a family of granulin-like repeats
The peptide was chemically synthesized using standard Fmoc chemistry and oxidized by air in solution, Cys17 and Cys27 were blocked with S-acetamidomethyl groups (Acm)
This structure was determined using standard 2D homonuclear techniques
structures with the least restraint violations
The structures are based on a total of 241 restraints, 174 are unambiguous NOE-derived distance constraints, 47 ambiguous NOE-derived distance constraints, 8 dihedral angle restraints, 10 distance restraints from hydrogen bonds, 2 distance restraints from disulfide bonds.
distance geometry and simulated annealing
0.5 mM HGA 1-31 (D1V, K3H, S9I, Q20P); 20 mM sodium acetate-d3, 10% D2O, 90% H2O
0.5 mM HGA 1-31 (D1V, K3H, S9I, Q20P); 20 mM sodium acetate-d3, 100% D2O
granulin/epithelin protein repeats, beta-hairpin stack, CYTOKINE
MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGT SSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCED RVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCC SDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIH CCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDH QHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGGTCCPSLGGSWACCQLPHAVCCEDRQH CCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCP AGFRCAARGTKCLRREAPRWDAPLRDPALRQLL