Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins.

Jayanthi, Lakshmi P; Mascarenhas, Nahren Manuel; Gosavi, Shachi

Jayanthi, Lakshmi P; Mascarenhas, Nahren Manuel; Gosavi, Shachi.

Jayanthi LP; Simons Centre for the Study of Living Machines, National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, 560065, India.
Mascarenhas NM; Department of Chemistry, Sacred Heart College (Autonomous), Tirupattur, 635601, India.
Gosavi S; Simons Centre for the Study of Living Machines, National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, 560065, India.

Curr Res Struct Biol ; 2: 180-190, 2020.

Article en En | MEDLINE | ID: mdl-34235478

Palabras clave

BI, Balancing interface; CS, conformational selection; CTD, C-terminal domain; Conformational selection; Dual structure based models; FEP, free energy profile; HisJ, histidine binding protein; IF, induced fit; Induced fit; MBP, maltose binding protein; MD simulations; MD, molecular dynamics; NTD, N-terminal domain; PBP, periplasmic binding protein; Periplasmic binding proteins; SH, spine helix; Structural restraints; WT, wild-type; dSBM, dual structure-based model; sSBM, single structure-based model

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Texto completo: 1 Banco de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Año: 2020 Tipo del documento: Article

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Texto completo: 1 Banco de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Año: 2020 Tipo del documento: Article