Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations
- Tokyo Metropolitan Inst. (Japan)
The interaction of mouse epidermal growth factor (mEGF) with micelles of a phospholipid analogue, perdeuterated dodecylphosphocholine (DPC), was investigated by two-dimensional {sup 1}H NMR. Sequence-specific resonance assignments of the micelle-bound mEGF have been made, and the chemical shifts were compared with those in the absence of DPC. DPC induced large chemical shift changes of the resonances from the residues in the C-terminal tail (residues 46-53) but little perturbation on the residues in the main core (residues 1-45). Starting from the three-dimensional structure in the absence of DPC, micelle-bound structures were calculated using the program XPLOR with interproton distance data obtained from NOESY spectra recorded in the presence of DPC. The C-terminal tail of mEGF was found to change conformation to form an amphiphilic structure when bound to the micelles. It is possible that induced fit in the C-terminal tail of mEGF occurs upon binding to a putative hydrophobic pocket of the EGF receptor.
- OSTI ID:
- 5559905
- Journal Information:
- Biochemistry; (United States), Vol. 31:3; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
GROWTH FACTORS
MOLECULAR STRUCTURE
PHOSPHOLIPIDS
NUCLEAR MAGNETIC RESONANCE
ANNEALING
DEUTERIUM COMPOUNDS
EPIDERMIS
MICELLAR SYSTEMS
ANIMAL TISSUES
BODY
EPITHELIUM
ESTERS
HEAT TREATMENTS
HYDROGEN COMPOUNDS
LIPIDS
MAGNETIC RESONANCE
MITOGENS
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
ORGANS
PROTEINS
RESONANCE
SKIN
TISSUES
550201* - Biochemistry- Tracer Techniques