Studies of the structure-activity relationships of peptides and proteins involved in growth and development based on their three-dimensional structures.
Peptides and proteins with similar amino acid sequences can have different biological functions. Knowledge of their three-dimensional molecular structures is critically important in identifying their functional determinants. In this review, I describe the results of our and other groups' structure-based functional characterization of insect insulin-like peptides, a crustacean hyperglycemic hormone-family peptide, a mammalian epidermal growth factor-family protein, and an intracellular signaling domain that recognizes proline-rich sequence.
Nagata
Koji
K
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan. aknagata@mail.ecc.u-tokyo.ac.jp
D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins; D004815:Epidermal Growth Factor / Q000737:chemistry / Q000378:metabolism; D007328:Insulin / Q000737:chemistry / Q000378:metabolism*; D007447:Invertebrate Hormones / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D020890:Neuregulin-1 / Q000737:chemistry / Q000378:metabolism*; D009479:Neuropeptides / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein; D013329:Structure-Activity Relationship
D060829:Arthropod Proteins; D007328:Insulin; D007447:Invertebrate Hormones; D009419:Nerve Tissue Proteins; D020890:Neuregulin-1; D009479:Neuropeptides; C015947:hyperglycemic hormone, crustacean; C012445:molt-inhibiting hormone; C075028:bombyxins; D004815:Epidermal Growth Factor