Thyroxine binding to type III iodothyronine deiodinase

Abstract Iodothyronine deiodinases (Dios) are important selenoproteins that control the concentration of the active thyroid hormone (TH) triiodothyronine through regioselective deiodination. The X-ray structure of a truncated monomer of Type III Dio (Dio3), which deiodinates TH inner rings through a selenocysteine (Sec) residue, revealed a thioredoxin-fold catalytic domain supplemented with an unstructured Ω-loop. Loop dynamics are driven by interactions of the conserved Trp207 with solvent in multi-microsecond molecular dynamics simulations of the Dio3 thioredoxin(Trx)-fold domain. Hydrogen bonding interactions of Glu200 with residues conserved across the Dio family anchor the loop’s N-terminus to the active site Ser-Cys-Thr-Sec sequence. A key long-lived loop conformation coincides with the opening of a cryptic pocket that accommodates thyroxine (T4) through an I⋯Se halogen bond to Sec170 and the amino acid group with a polar cleft. The Dio3-T4 complex is stabilized by an I⋯O halogen bond between an outer ring iodine and Asp211, consistent with Dio3 selectivity for inner ring deiodination. Non-conservation of residues, such as Asp211, in other Dio types in the flexible portion of the loop sequence suggests a mechanism for regioselectivity through Dio type-specific loop conformations. Cys168 is proposed to attack the selenenyl iodide intermediate to regenerate Dio3 based upon structural comparison with related Trx-fold proteins.

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Atomistic understanding on molecular halide perovskite/organic/TiO2 interface with bifunctional interfacial modifier: A case study on halogen bond and carboxylic acid group

Applied Surface Science ◽

10.1016/j.apsusc.2019.144274 ◽

2020 ◽

Vol 502 ◽

pp. 144274

Author(s):

Lei Zhang ◽

Yuxiao Chen

Keyword(s):

Carboxylic Acid ◽

Halogen Bond ◽

Acid Group ◽

Carboxylic Acid Group ◽

Halide Perovskite ◽

Interfacial Modifier

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Acute pretranslational regulation of type III iodothyronine deiodinase by growth hormone and dexamethasone in chicken embryos

Molecular and Cellular Endocrinology ◽

10.1016/s0303-7207(98)00218-4 ◽

1999 ◽

Vol 147 (1-2) ◽

pp. 49-56 ◽

Cited By ~ 37

Author(s):

Serge Van der Geyten ◽

Nadine Buys ◽

Jo P. Sanders ◽

Eddy Decuypere ◽

Theo J. Visser ◽

...

Keyword(s):

Growth Hormone ◽

Iodothyronine Deiodinase ◽

Chicken Embryos ◽

Type Iii

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Model-based optimal attitude and positioning control of small-scale unmanned helicopter

Robotica ◽

10.1017/s026357470400092x ◽

2005 ◽

Vol 23 (1) ◽

pp. 51-63 ◽

Cited By ~ 62

Author(s):

Jinok Shin ◽

Kenzo Nonami ◽

Daigo Fujiwara ◽

Kensaku Hazawa

Keyword(s):

Network Theory ◽

Attitude Control ◽

Position Control ◽

Small Scale ◽

Unmanned Helicopter ◽

Positioning Control ◽

Model Based ◽

Loop Dynamics ◽

Neural Network Theory ◽

Dynamics Simulations

In this paper, we propose a model-based control system design for autonomous flight and guidance control of a small-scale unmanned helicopter. Small-scale unmanned helicopters have been studied by way of fuzzy and neural network theory, but control that is not based on a model fails to yield good stabilization performance. For this reason, we design a mathematical model and a model-based controller for a small-scale unmanned helicopter system. In order to realize a fully autonomous small-scale unmanned helicopter, we have designed a MIMO attitude controller and a trajectory controller equipped with a Kalman filter-based LQI for a small-scale unmanned helicopter. The design of the trajectory controller takes into consideration the characteristics of attitude closed-loop dynamics. Simulations and experiments have shown that the proposed scheme for attitude control and position control is very useful.

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Watkins, Prof. Jeffrey Clifton, (born 20 Dec. 1929), Hon. Professor of Pharmacology, 1989–99, and Leader of Excitatory Amino Acid Group, Department of Pharmacology, 1973–99, School of Medical Sciences (formerly The Medical School), Bristol (Hon. Senior Research Fellow, 1983–89), now Professor Emeritus

10.1093/ww/9780199540884.013.39015 ◽

2007 ◽

Keyword(s):

Amino Acid ◽

Medical School ◽

Excitatory Amino Acid ◽

Acid Group ◽

Professor Emeritus ◽

Medical Sciences ◽

Amino Acid Group ◽

Research Fellow ◽

Senior Research Fellow ◽

Senior Research

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Watkins, Prof. Jeffrey Clifton, (born 20 Dec. 1929), Hon. Professor of Pharmacology, 1989–99, and Leader of Excitatory Amino Acid Group, Department of Pharmacology, 1973–99, School of Medical Sciences (formerly The Medical School), Bristol (Hon. Senior Research Fellow, 1983–89), now Professor Emeritus

10.1093/ww/9780199540884.013.u39015 ◽

2007 ◽

Keyword(s):

Amino Acid ◽

Medical School ◽

Excitatory Amino Acid ◽

Acid Group ◽

Professor Emeritus ◽

Medical Sciences ◽

Amino Acid Group ◽

Research Fellow ◽

Senior Research Fellow ◽

Senior Research

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Stability Constants of Some Metal Complexes Formed by Mimosine and Related Compounds

Australian Journal of Chemistry ◽

10.1071/ch9790021 ◽

1979 ◽

Vol 32 (1) ◽

pp. 21 ◽

Cited By ~ 24

Author(s):

H Stunzi ◽

DD Perrin ◽

T Teitei ◽

RLN Harris

Keyword(s):

Amino Acid ◽

Stability Constants ◽

Metal Binding ◽

Acid Group ◽

Biologically Active ◽

Amino Acid Group ◽

Dimeric Complexes ◽

Major Species ◽

Active Amino Acid ◽

Related Compounds

Complex formation of the biologically active amino acid L-mimosine [α-amino-β-(3-hydroxy-4-oxo-1,4-dihydropyridin-1-yl)propanoic acid (1)], mimosinic acid (2), mimosine methyl ether (9) and 3-hydroxy-1-methylpyridin-4(1H)-one (4) with Cu2+, Zn2+, Cd2+ and Pb2+ was studied. Stability constants were determined by potentiometric titration in 0.15M KNOB3 as inert electrolyte at 37�. In the monomeric complexes formed by the mimosine derivatives, metal binding by the hydroxypyridone moiety was favoured relative to the amino acid group. With mimosine, dimeric complexes were major species. Under physiological conditions, mimosine binds copper and zinc ions more strongly than do simpler amino acids.

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Reversible Oxygenation ofα-Amino Acid–Cobalt(II) Complexes

Bioinorganic Chemistry and Applications ◽

10.1155/2016/3585781 ◽

2016 ◽

Vol 2016 ◽

pp. 1-10 ◽

Cited By ~ 2

Author(s):

Xincun Zhang ◽

Fan Yue ◽

Hui Li ◽

Yan Huang ◽

Yi Zhang ◽

...

Keyword(s):

Amino Acid ◽

Time Lapse ◽

Acid Group ◽

Oxygen Electrode ◽

Oxygen Carriers ◽

Amino Acid Group ◽

Specific Configuration ◽

Reversible Formation ◽

Hydroxy Groups ◽

The Relationship

We systematically investigated the reversibility, time lapse, and oxygenation-deoxygenation properties of 15 naturalα-amino acid–Co(II) complexes through UV-vis spectrophotometer, polarographic oxygen electrode, and DFT calculations, respectively, to explore the relationship between the coordinating structure and reversible oxygenation ofα-amino acid–Co(II) complexes. Results revealed that theα-amino acid structure plays a key role in the reversible oxygenation properties of these complexes. The specific configuration of theα-amino acid group affects theeg1electron of Co(II) transfer to theπ⁎orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co–O2bond when O2coordinates with Co(II) complexes. Therefore, the co-coordination of amino and carboxyl groups is a determinant of Co complexes to absorb O2reversibly. The group adjacent to theα-amino acid unit evidently influences the dioxygen affinity and antioxidation ability of the complexes. The presence of amino (or imino) and hydroxy groups adjacent to theα-amino acid group increases the oxygenation-deoxygenation rate and the number of reversible cycles. Our findings demonstrate a new mechanism to develop reversible oxygenation complexes and to reveal the oxygenation of oxygen carriers.

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Cytosolic interaction of type III human CD38 with CIB1 modulates cellular cyclic ADP-ribose levels

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1703718114 ◽

2017 ◽

Vol 114 (31) ◽

pp. 8283-8288 ◽

Cited By ~ 24

Author(s):

Jun Liu ◽

Yong Juan Zhao ◽

Wan Hua Li ◽

Yun Nan Hou ◽

Ting Li ◽

...

Keyword(s):

Catalytic Domain ◽

Bimolecular Fluorescence Complementation ◽

Knock Out ◽

Guide Rna ◽

Type Iii ◽

Cyclic Adp Ribose ◽

Human Multiple Myeloma ◽

Hybrid Screening

CD38 catalyzes the synthesis of the Ca2+ messenger, cyclic ADP-ribose (cADPR). It is generally considered to be a type II protein with the catalytic domain facing outside. How it can catalyze the synthesis of intracellular cADPR that targets the endoplasmic Ca2+ stores has not been resolved. We have proposed that CD38 can also exist in an opposite type III orientation with its catalytic domain facing the cytosol. Here, we developed a method using specific nanobodies to immunotarget two different epitopes simultaneously on the catalytic domain of the type III CD38 and firmly established that it is naturally occurring in human multiple myeloma cells. Because type III CD38 is topologically amenable to cytosolic regulation, we used yeast-two-hybrid screening to identify cytosolic Ca2+ and integrin-binding protein 1 (CIB1), as its interacting partner. The results from immunoprecipitation, ELISA, and bimolecular fluorescence complementation confirmed that CIB1 binds specifically to the catalytic domain of CD38, in vivo and in vitro. Mutational studies established that the N terminus of CIB1 is the interacting domain. Using shRNA to knock down and Cas9/guide RNA to knock out CIB1, a direct correlation between the cellular cADPR and CIB1 levels was demonstrated. The results indicate that the type III CD38 is functionally active in producing cellular cADPR and that the activity is specifically modulated through interaction with cytosolic CIB1.

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