دورية أكاديمية
Molecular and structural analysis of a mechanical transition of helices in the L. donovani coronin coiled-coil domain.
| العنوان: | Molecular and structural analysis of a mechanical transition of helices in the L. donovani coronin coiled-coil domain. |
|---|---|
| المؤلفون: | Karade SS; Molecular and Structural Biology Division, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, Uttar Pradesh, India., Ansari A; Molecular and Structural Biology Division, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, Uttar Pradesh, India., Srivastava VK; Molecular and Structural Biology Division, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, Uttar Pradesh, India., Nayak AR; Molecular and Structural Biology Division, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, Uttar Pradesh, India., Pratap JV; Molecular and Structural Biology Division, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, Uttar Pradesh, India. Electronic address: jvpratap@cdri.res.in. |
| المصدر: | International journal of biological macromolecules [Int J Biol Macromol] 2020 Jan 15; Vol. 143, pp. 785-796. Date of Electronic Publication: 2019 Nov 25. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: Guildford, Eng., IPC Science and Technology Press. |
| مواضيع طبية MeSH: | Leishmania/*metabolism , Microfilament Proteins/*chemistry , Microfilament Proteins/*metabolism, Amino Acid Sequence ; Animals ; Cattle ; Models, Molecular ; Mutant Proteins/chemistry ; Protein Domains ; Protein Multimerization ; Protein Structure, Secondary |
| مستخلص: | Protein-protein interactions of cellular importance are mediated by coiled coils (CCs), the ubiquitous structural motif formed by the association of two or more α-helices in a knobs into holes manner. Coronins, actin-associated multi-functional proteins that possess distinct cytoskeleton-dependent and independent functions, oligomerize through their C-terminal CC domain. The structure of the L. donovani coronin CC domain (LdCoroCC; PDB ID 5CX2) revealed, in addition to a novel topology and architecture, an inherent asymmetry, with one of the helices of the 4-helix bundle axially shifted (~2 turns). The structural analysis identified that steric hindrance by Ile 486, Leu 493 and Met 500 as the cause for this asymmetry. To experimentally validate this hypothesis and to better understand the sequence-structure relationship in CCs, these amino acids have been mutated (I486A, L493A, M500V and the double mutant I486A-L493A) and characterized. Thermal CD studies suggest that the I486A and M500V mutants have comparable T (Copyright © 2019 Elsevier B.V. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Asymmetry-symmetry transition; Coronin- coiled-coil; Leishmania donovani |
| المشرفين على المادة: | 0 (Microfilament Proteins) 0 (Mutant Proteins) 145420-64-0 (coronin proteins) |
| تواريخ الأحداث: | Date Created: 20191129 Date Completed: 20200930 Latest Revision: 20200930 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1016/j.ijbiomac.2019.09.138 |
| PMID: | 31778699 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1879-0003 |
|---|---|
| DOI: | 10.1016/j.ijbiomac.2019.09.138 |