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- SASDDT8: Neural/ectodermal development factor IMP-L2 in complex with insul... -

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Basic information

Entry
Database: SASBDB / ID: SASDDT8
SampleNeural/ectodermal development factor IMP-L2 in complex with insulin-like peptide 5 (DILP5)
  • Insulin-like peptide 5 (protein), Drosophila melanogaster
  • Neural/ectodermal development factor IMP-L2 (protein), Imp-L2 IBP, Drosophila melanogaster
Function / homology
Function and homology information


positive regulation of entry into reproductive diapause / response to insect / dendrite self-avoidance / cell-cell adhesion mediator activity / insulin binding / response to starvation / homophilic cell adhesion via plasma membrane adhesion molecules / negative regulation of lipid storage / positive regulation of insulin receptor signaling pathway / negative regulation of insulin receptor signaling pathway ...positive regulation of entry into reproductive diapause / response to insect / dendrite self-avoidance / cell-cell adhesion mediator activity / insulin binding / response to starvation / homophilic cell adhesion via plasma membrane adhesion molecules / negative regulation of lipid storage / positive regulation of insulin receptor signaling pathway / negative regulation of insulin receptor signaling pathway / axon guidance / determination of adult lifespan / hormone activity / axon / extracellular space / extracellular region / plasma membrane
Similarity search - Function
Insulin-related peptide, invertebrates / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin family signature. / Insulin-like superfamily / Immunoglobulin I-set / Immunoglobulin I-set domain ...Insulin-related peptide, invertebrates / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin family signature. / Insulin-like superfamily / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Insulin-like peptide 5 / Neural/ectodermal development factor IMP-L2
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
CitationJournal: Nat Commun / Year: 2018
Title: Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones.
Authors: Nikolaj Kulahin Roed / Cristina M Viola / Ole Kristensen / Gerd Schluckebier / Mathias Norrman / Waseem Sajid / John D Wade / Asser Sloth Andersen / Claus Kristensen / Timothy R Ganderton / ...Authors: Nikolaj Kulahin Roed / Cristina M Viola / Ole Kristensen / Gerd Schluckebier / Mathias Norrman / Waseem Sajid / John D Wade / Asser Sloth Andersen / Claus Kristensen / Timothy R Ganderton / Johan P Turkenburg / Pierre De Meyts / Andrzej M Brzozowski /
Abstract: The insulin/insulin-like growth factor signalling axis is an evolutionary ancient and highly conserved hormonal system involved in the regulation of metabolism, growth and lifespan in animals. Human ...The insulin/insulin-like growth factor signalling axis is an evolutionary ancient and highly conserved hormonal system involved in the regulation of metabolism, growth and lifespan in animals. Human insulin is stored in the pancreas, while insulin-like growth factor-1 (IGF-1) is maintained in blood in complexes with IGF-binding proteins (IGFBP1-6). Insect insulin-like polypeptide binding proteins (IBPs) have been considered as IGFBP-like structural and functional homologues. Here, we report structures of the Drosophila IBP Imp-L2 in its free form and bound to Drosophila insulin-like peptide 5 and human IGF-1. Imp-L2 contains two immunoglobulin-like fold domains and its architecture is unrelated to human IGFBPs, suggesting a distinct strategy for bioavailability regulation of insulin-like hormones. Similar hormone binding modes may exist in other insect vectors, as the IBP sequences are highly conserved. Therefore, these findings may open research routes towards a rational interference of transmission of diseases such as malaria, dengue and yellow fevers.
Contact author
  • Mathias Norrman (Novo Nordisk A/S)

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Structure visualization

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Models

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Sample

SampleName: Neural/ectodermal development factor IMP-L2 in complex with insulin-like peptide 5 (DILP5)
Specimen concentration: 2.30-9.30 / Entity id: 1135 / 1154
BufferName: phosphate buffered saline / pH: 7.4
Entity #1135Type: protein / Description: Insulin-like peptide 5 / Formula weight: 5.385 / Num. of mol.: 1 / Source: Drosophila melanogaster / References: UniProt: E7BBS4
Sequence:
NSLRACGPAL MDMLRVACPN GFNSMFAKGV VDSCCRKSCS FSTLRAYCDS
Entity #1154Name: Imp-L2 IBP / Type: protein / Description: Neural/ectodermal development factor IMP-L2 / Formula weight: 29.895 / Num. of mol.: 1 / Source: Drosophila melanogaster / References: UniProt: Q09024
Sequence: MEAKMNLHVC ALALLLFGSI ATVRGRAVDL VDDSNDVDNS IEAEEEKPRN RAFEADWLKF TKTPPTKLQQ ADGATIEIVC EMMGSQVPSI QWVVGHLPRS ELDDLDSNQV AEEAPSAIVR VRSSHIIDHV LSEARTYTCV GRTGSKTIYA STVVHPPRSS RLTPEKTYPG ...Sequence:
MEAKMNLHVC ALALLLFGSI ATVRGRAVDL VDDSNDVDNS IEAEEEKPRN RAFEADWLKF TKTPPTKLQQ ADGATIEIVC EMMGSQVPSI QWVVGHLPRS ELDDLDSNQV AEEAPSAIVR VRSSHIIDHV LSEARTYTCV GRTGSKTIYA STVVHPPRSS RLTPEKTYPG AQKPRIIYTE KTHLDLMGSN IQLPCRVHAR PRAEITWLNN ENKEIVQGHR HRVLANGDLL ISEIKWEDMG NYKCIARNVV GKDTADTFVY PVLNEED

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Experimental information

BeamInstrument name: ESRF ID14-3 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.093 Å / Dist. spec. to detc.: 2.43 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: Neural/ectodermal development factor IMP-L2 complexed with insulin-like peptide 5 (DILP5)
Measurement date: Nov 20, 2011 / Storage temperature: 5 °C / Cell temperature: 25 °C / Exposure time: 10 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0645 6.1076
ResultType of curve: merged /
ExperimentalStandardPorod
MW30 kDa30 kDa-
Volume--55 nm3

GuinierGuinier error
Forward scattering, I044.77 0.03
Radius of gyration, Rg2.59 nm0.04

MinMax
D-9
Guinier point26 65

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