دورية أكاديمية
أعرض في EDS

Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction.

التفاصيل البيبلوغرافية
العنوان: Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction.
المؤلفون: Parihar PS; Division of Biochemistry and Structural Biology, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow, 226031, Uttar Pradesh, India., Singh A; Division of Biochemistry and Structural Biology, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow, 226031, Uttar Pradesh, India., Karade SS; Division of Biochemistry and Structural Biology, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow, 226031, Uttar Pradesh, India., Sahasrabuddhe AA; Division of Biochemistry and Structural Biology, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow, 226031, Uttar Pradesh, India., Pratap JV; Division of Biochemistry and Structural Biology, CSIR - Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow, 226031, Uttar Pradesh, India.
المصدر: Current research in structural biology [Curr Res Struct Biol] 2021 Oct 14; Vol. 3, pp. 268-276. Date of Electronic Publication: 2021 Oct 14 (Print Publication: 2021).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier B.V Country of Publication: Netherlands NLM ID: 101767537 Publication Model: eCollection Cited Medium: Internet ISSN: 2665-928X (Electronic) Linking ISSN: 2665928X NLM ISO Abbreviation: Curr Res Struct Biol Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: [Amsterdam] : Elsevier B.V., [2019]-
مستخلص: The two-domain actin associated protein coronin interacts with filamentous (F-) actin, facilitating diverse biological processes including cell proliferation, motility, phagocytosis, host-parasite interaction and cargo binding. The conserved N-terminal β-propeller domain is involved in protein: protein interactions, while the C-terminal coiled-coil domain mediates oligomerization, transducing conformational changes. The L. donovani coronin coiled-coil (LdCoroCC) domain exhibited a novel topology and oligomer association with an inherent asymmetry, caused primarily by three a residues of successive heptads. In the T.brucei homolog (TbrCoro), two of these ' a' residues are different (Val 493 & 507 replacing LdCoroCC Ile 486 and Met 500 respectively). The elucidated structure possesses a similar topology and assembly while comparative structural analysis shows that the T.brucei coronin coiled-coil domain (TbrCoroCC) too possesses the asymmetry though its magnitude is smaller. Analysis identifies that the asymmetric state is stabilized via cyclic salt bridges formed by Arg 497 and Glu 504. Co-localization studies (LdCoro, TbrCoro and corresponding mutant coiled coil constructs) with actin show that there are subtle differences in their binding patterns, with the double mutant V493I-V507M showing maximal effect. None of the constructs have an effect on F-actin length. Taken together with LdCoroCC, we therefore conclude that the inherent asymmetric structures are essential for kinetoplastids, and are of interest in understanding and exploiting actin dynamics.
Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(© 2021 The Authors.)
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فهرسة مساهمة: Keywords: Actin; Coronin; Crystal structure; In vivo imaging; Leishmania; Oligomerization; Trypanosoma brucei
تواريخ الأحداث: Date Created: 20211108 Latest Revision: 20231108
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8554105
DOI: 10.1016/j.crstbi.2021.10.002
PMID: 34746809
قاعدة البيانات: MEDLINE
الوصف
تدمد:2665-928X
DOI:10.1016/j.crstbi.2021.10.002