Study of the Molecular Recognition Mechanism of an Ultrathin MIP Film-Based Chiral Electrochemical Sensor

2016 ◽  
Vol 217 ◽  
pp. 195-202 ◽  
Author(s):  
Bogdan-Cezar Iacob ◽  
Ede Bodoki ◽  
Cosmin Farcau ◽  
Lucian Barbu-Tudoran ◽  
Radu Oprean
Keyword(s):  
Molecular Recognition ◽  
Electrochemical Sensor ◽  
Recognition Mechanism

scholarly journals X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Lan Guan ◽  
Parameswaran Hariharan
Keyword(s):  
Molecular Recognition ◽  
Binding Pocket ◽  
Cation Binding ◽  
Recognition Mechanism ◽  
X Ray ◽  
X Ray Crystallography ◽  
Sugar Binding ◽  
Sugar Specificity ◽  
Major Facilitator ◽  
Mfs Transporters

AbstractMajor facilitator superfamily_2 transporters are widely found from bacteria to mammals. The melibiose transporter MelB, which catalyzes melibiose symport with either Na+, Li+, or H+, is a prototype of the Na+-coupled MFS transporters, but its sugar recognition mechanism has been a long-unsolved puzzle. Two high-resolution X-ray crystal structures of a Salmonella typhimurium MelB mutant with a bound ligand, either nitrophenyl-α-d-galactoside or dodecyl-β-d-melibioside, were refined to a resolution of 3.05 or 3.15 Å, respectively. In the substrate-binding site, the interaction of both galactosyl moieties on the two ligands with MelBSt are virturally same, so the sugar specificity determinant pocket can be recognized, and hence the molecular recognition mechanism for sugar binding in MelB has been deciphered. The conserved cation-binding pocket is also proposed, which directly connects to the sugar specificity pocket. These key structural findings have laid a solid foundation for our understanding of the cooperative binding and symport mechanisms in Na+-coupled MFS transporters, including eukaryotic transporters such as MFSD2A.

Preparation of molecularly imprinted polymer for sinomenine and study on its molecular recognition mechanism

Polymer ◽  
2006 ◽  
Vol 47 (11) ◽  
pp. 3792-3798 ◽  
Author(s):  
Li-Qin Lin ◽  
Ying-Chun Li ◽  
Qiang Fu ◽  
Lang-Chong He ◽  
Jing Zhang ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Molecularly Imprinted Polymer ◽  
Imprinted Polymer ◽  
Recognition Mechanism ◽  
Molecularly Imprinted

scholarly journals Molecular Recognition Mechanism of Calmodulin Examined by Perturbation-Response Scanning

2011 ◽  
Vol 100 (3) ◽  
pp. 534a
Author(s):  
Canan Atilgan ◽  
A. Ozlem Aykut ◽  
Ali Rana Atilgan
Keyword(s):  
Molecular Recognition ◽  
Recognition Mechanism

Production of anti-amoxicillin ScFv antibody and simulation studying its molecular recognition mechanism for penicillins

2016 ◽  
Vol 51 (11) ◽  
pp. 742-750 ◽  
Author(s):  
Jing Liu ◽  
Hui C. Zhang ◽  
Chang F. Duan ◽  
Jun Dong ◽  
Guo X. Zhao ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Scfv Antibody ◽  
Recognition Mechanism

scholarly journals Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Luigi Russo ◽  
Karin Giller ◽  
Edith Pfitzner ◽  
Christian Griesinger ◽  
Stefan Becker
Keyword(s):  
Molecular Recognition ◽  
Recognition Mechanism ◽  
Insight Into

scholarly journals Molecular recognition of sugar binding in a melibiose transporter MelB by X-ray crystallography

2020 ◽  
Author(s):  
Lan Guan ◽  
Parameswaran Hariharan
Keyword(s):  
Molecular Recognition ◽  
Binding Site ◽  
Crystal Structures ◽  
Mammalian Cells ◽  
Substrate Binding ◽  
Structural Basis ◽  
Cooperative Binding ◽  
Recognition Mechanism ◽  
Substrate Binding Site ◽  
X Ray

AbstractThe symporter melibiose permease MelB is the best-studied representative from MFS_2 family and the only protein in this large family with crystal structure determined. Previous thermodynamic studies show that MelB utilizes a cooperative binding as the core mechanism for its obligatory symport. Here we present two sugar-bound X-ray crystal structures of a Salmonella typhimurium MelB D59C uniport mutant that binds and catalyzes melibiose transport uncoupled to either cation, as determined by biochemical and biophysical characterizations. The two structures with bound nitrophenyl-α-D-galactoside or dodecyl-β-D-melibioside, which were refined to a resolution of 3.05 or 3.15 Å, respectively, are virtually identical at an outward-facing conformation; each one contains a α-galactoside molecule in the middle of protein. In the substrate-binding site, the galactosyl moiety on both ligands are at an essentially same configuration, so a galactoside specificity determinant pocket can be recognized, and hence the molecular recognition mechanism for the binding of sugar in MelB is deciphered. The data also allow to assign the conserved cation-binding pocket, which is directly connected to the sugar specificity determinant pocket. The intimate connection between the two selection sites lays the structural basis for the cooperative binding and coupled transport. This key structural finding answered the long-standing question on the substrate binding for the Na+-coupled MFS family of transporters.SignificanceMajor facilitator superfamily_2 transporters contain >10,000 members that are widely expressed from bacteria to mammalian cells, and catalyze uptake of varied nutrients from sugars to phospholipids. While several crystal structures with bound sugar for other MFS permeases have been determined, they are either uniporters or symporters coupled solely to H+. MelB catalyzes melibiose symport with either Na+, Li+, or H+, a prototype for Na+-coupled MFS transporters, but its sugar recognition has been a long-unsolved puzzle. Two high-resolution crystal structures presented here clearly reveal the molecular recognition mechanism for the binding of sugar in MelB. The substrate-binding site is characterized with a small specificity groove adjoining a large nonspecific cavity, which could offer a potential for future exploration of active transporters for drug delivery.

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