Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement
| العنوان: | Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement |
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| المؤلفون: | Julie Ménétrey, Paola Llinas, Annélie de Régibus, Mélanie Chenon, Cátia Moreira, Pedro A. Fernandes, T. Quyen Nguyen, Maria J. Ramos, Raphael Guerois, Aline Coquard |
| المساهمون: | Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), Centre National de la Recherche Scientifique (CNRS), Faculty of Science and Technology, BIOSCOPE Group, UCIBIO-REQUIMTE, Universidade de Lisboa (ULISBOA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Requimte, Departamento de Química (DQ), Faculdade de Ciências e Tecnologia = School of Science & Technology (FCT NOVA), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Faculdade de Ciências e Tecnologia = School of Science & Technology (FCT NOVA), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade do Porto, Laboratoire d'Enzymologie et Biochimie Structurales ( LEBS ), Centre National de la Recherche Scientifique ( CNRS ), Universidade de Lisboa ( ULISBOA ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Requimente, Departamento de Química, Faculdade de Ciências, Universidade do Porto [Porto], Universidade de Lisboa = University of Lisbon (ULISBOA), Universidade do Porto = University of Porto-Departamento de Química (DQ), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA) |
| المصدر: | Acta crystallographica. Section F, Structural biology communications Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩ Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. 〈10.1107/S2053230X16001576〉 Acta crystallographica Section F : Structural biology communications [2014-...] Acta crystallographica Section F : Structural biology communications [2014-..], 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩ |
| بيانات النشر: | HAL CCSD, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Leucine zipper, crystal structure, buried asparagine, Stereochemistry, [SDV]Life Sciences [q-bio], Biophysics, Nerve Tissue Proteins, Small G Protein, Plasma protein binding, Molecular Dynamics Simulation, Crystallography, X-Ray, Antiparallel (biochemistry), Biochemistry, Protein Structure, Secondary, Research Communications, 03 medical and health sciences, Structural Biology, leucine zipper II, Genetics, Molecular motor, Humans, JIP4, Protein Interaction Domains and Motifs, Amino Acid Sequence, Binding site, Structural motif, Adaptor Proteins, Signal Transducing, JIP3, antiparallel coiled coil, Coiled coil, Leucine Zippers, 030102 biochemistry & molecular biology, [ SDV ] Life Sciences [q-bio], Chemistry, Condensed Matter Physics, Peptide Fragments, molecular dynamics, Protein Structure, Tertiary, Crystallography, 030104 developmental biology, Crystallization |
| الوصف: | International audience; JIP3 and JIP4, two highly related scaffolding proteins for MAP kinases, are binding partners for two molecular motors as well as for the small G protein ARF6. The leucine zipper II (LZII) region of JIP3/4 is the binding site for these three partners. Previously, the crystal structure of ARF6 bound to JIP4 revealed LZII in a parallel coiled-coil arrangement. Here, the crystal structure of an N-terminally truncated form of LZII of JIP3 alone shows an unexpected antiparallel arrangement. Using molecular dynamics and modelling, the stability of this antiparallel LZII arrangement, as well as its specificity for ARF6, were investigated. This study highlights that N-terminal truncation of LZII can change its coiled-coil orientation without affecting its overall stability. Further, a conserved buried asparagine residue was pinpointed as a possible structural determinant for this dramatic structural rearrangement. Thus, LZII of JIP3/4 is a versatile structural motif, modifications of which can impact partner recognition and thus biological function. |
| اللغة: | English |
| تدمد: | 2053-230X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0893bc1f8ae40cb11b2669939786237Test https://hal.archives-ouvertes.fr/hal-01457789Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....f0893bc1f8ae40cb11b2669939786237 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 2053230X |
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