Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein

Journal Article · Tue May 14 00:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00233a020· OSTI ID:5510638

Rosen, M K; Michnick, S W; Karplus, M; Schreiber, S L ^[1]

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1. Harvard Univ., Cambridge, MA (USA)

Sequential {sup 1}H and {sup 15}N assignments of human FKBP, a cytosolic binding protein for the immunosuppressive agents FK506 and rapamycin, are reported. A combination of homonuclear and relayed heteronuclear experiments has enabled assignment of 98 of 99 backbone amide NHs, 119 of 120 C{sup {alpha}}Hs, 97 of 99 non-proline amide {sup 15}Ns, and 375 of 412 side-chain resonances of this 107-residue protein. Long-range NOEs are used to demonstrate that FKBP has a novel folding topology consisting of a five-stranded antiparallel {beta} sheet with +3, +1, {minus}3, +1 loop connectivity.

• OSTI ID: 5510638
• Journal Information: Biochemistry; (United States), Vol. 30:19; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ANTIBIOTICS
NUCLEAR MAGNETIC RESONANCE
IMMUNOSUPPRESSIVE DRUGS
CROSS-LINKING
MEMBRANE PROTEINS
MAN
MOLECULAR STRUCTURE
NITROGEN 15
OVERHAUSER EFFECT
PROTONS
PURIFICATION
ANIMALS
ANTI-INFECTIVE AGENTS
BARYONS
CHEMICAL REACTIONS
DRUGS
ELEMENTARY PARTICLES
FERMIONS
HADRONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MAMMALS
NITROGEN ISOTOPES
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
POLYMERIZATION
PRIMATES
PROTEINS
RESONANCE
STABLE ISOTOPES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques