Metal-polypeptide interactions: The conformational state of iron proteins

Llinás, Miguel

doi:10.1007/bfb0113665

Cited by 34 publications

(10 citation statements)

References 288 publications

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“…Further experimental crystal structure study should be necessary to explain this AXL alternative splicing effects. Generally, dynamic kinetics and biological function of a specific signaling pathway could be changed depending on interaction between receptor and its ligand as well as their domain folding structure [ 26 ]. Therefore, the different 3D structures of the alternative AXL isoforms may be related to regulatory mechanism of signaling cascade.…”

Section: Resultsmentioning

confidence: 99%

Molecular analysis of alternative transcripts of equine AXL receptor tyrosine kinase gene

Park

Song

Kim

et al. 2017

Asian-Australas J Anim Sci

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ObjectiveSince athletic performance is a most importance trait in horses, most research focused on physiological and physical studies of horse athletic abilities. In contrast, the molecular analysis as well as the regulatory pathway studies remain insufficient for evaluation and prediction of horse athletic abilities. In our previous study, we identified AXL receptor tyrosine kinase (AXL) gene which was expressed as alternative spliced isoforms in skeletal muscle during exercise. In the present study, we validated two AXL alternative splicing transcripts (named as AXLa for long form and AXLb for short form) in equine skeletal muscle to gain insight(s) into the role of each alternative transcript during exercise.MethodsWe validated two isoforms of AXL transcripts in horse tissues by reverse transcriptase polymerase chain reaction (RT-PCR), and then cloned the transcripts to confirm the alternative locus and its sequences. Additionally, we examined the expression patterns of AXLa and AXLb transcripts in horse tissues by quantitative RT-PCR (qRT-PCR).ResultsBoth of AXLa and AXLb transcripts were expressed in horse skeletal muscle and the expression levels were significantly increased after exercise. The sequencing analysis showed that there was an alternative splicing event at exon 11 between AXLa and AXLb transcripts. 3-dimentional (3D) prediction of the alternative protein structures revealed that the structural distance of the connective region between fibronectin type 3 (FN3) and immunoglobin (Ig) domain was different between two alternative isoforms.ConclusionIt is assumed that the expression patterns of AXLa and AXLb transcripts would be involved in regulation of exercise-induced stress in horse muscle possibly through an NF-κB signaling pathway. Further study is necessary to uncover biological function(s) and significance of the alternative splicing isoforms in race horse skeletal muscle.

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Section: Resultsmentioning

confidence: 99%

Molecular analysis of alternative transcripts of equine AXL receptor tyrosine kinase gene

Park

Song

Kim

et al. 2017

Asian-Australas J Anim Sci

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“…We first examine the structure of our model hexapeptide molecule, HPM, in the gas phase. In a snapshot shown in Figure 1, the employed force field for the model peptide yields a nearly cyclic structure analogous to the native structure for ferrichrome-type siderphores, 21 of which the amino terminal of SER2 and carboxyl terminal of LYS1 are linked together. End-to-end distance between the N-terminal and C-terminal, l e , is 3.2 Å.…”

Section: Resultsmentioning

confidence: 99%

“…As a model protein we consider a small metal-binding peptide molecule, commonly found in siderochromes, compounds typically found in bacteria and fungi and are involved in the iron transport process of microbial organisms. 21 The key and common structural motif in siderochromes are ferrichromes. Ferrichrome is a small peptide molecule, composed of six residues arranged in a cyclic hexapeptide structure, and it acts as a strong ferric chelator.…”

Section: Introductionmentioning

confidence: 99%

Solvation of a Small Metal-Binding Peptide in Room-Temperature Ionic Liquids

Shim¹,

Kim

Jung

2012

Bulletin of the Korean Chemical Society

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Structural properties of a small hexapeptide molecule modeled after metal-binding siderochrome immersed in a room-temperature ionic liquid (RTIL) are studied via molecular dynamics simulations. We consider two different RTILs, each of which is made up of the same cationic species, 1-butyl-3-methylimidazolium (BMI + ), but different anions, hexafluorophosphate (PF6 − ) and chloride (Cl − ). We investigate how anionic properties such as hydrophobicity/hydrophilicity or hydrogen bonding capability affect the stabilization of the peptide in RTILs. To examine the effect of peptide-RTIL electrostatic interactions on solvation, we also consider a hypothetical solvent BMI − . This is ascribed to the good hydrogen-bond accepting power of chloride anions, which enables them to bind strongly to hydroxyl groups of the peptide and to stabilize its structure. Transport properties of the peptide are examined briefly. Translations of the peptide significantly slow down in highly viscous RTILs.

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“…A smaller molecule, myohemerythrin, related to the subunit of hemerythrin, is found in the muscle tissue of organisms containing the octamer, analogous to the hemoglobin-myoglobin system found in most other organisms. Extensive discussions of the biochemistry of these molecules can be found in review articles by Klotz (1971), Llinas (1973), and Klotz, Klippenstein & Hendrickson (1976).…”

Section: Introductionmentioning

confidence: 99%

Difference Fourier refinement of metaquohemerythrin

Stenkamp¹,

Sieker²,

Jensen³

1978

Acta Cryst Sect A

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A model for metaquohemerythrin from Themiste dyscritum has been refined in the crystallographic sense of the term by difference Fourier methods at 2.8 and 2.5 ,/~ resolution. Fourteen cycles of refinement reduced R from an initial value of 0.385 for the 9461 reflections from I0 to 2.8/k to 0.253 for 16 363 reflections from 10 to 2-5 A resolution. On the basis of peaks in difference maps, 49 water molecules have been added to the model for a total of 3833 atoms in the asymmetric unit.

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Metal-polypeptide interactions: The conformational state of iron proteins

Cited by 34 publications

References 288 publications

Molecular analysis of alternative transcripts of equine AXL receptor tyrosine kinase gene

Molecular analysis of alternative transcripts of equine AXL receptor tyrosine kinase gene

Solvation of a Small Metal-Binding Peptide in Room-Temperature Ionic Liquids

Difference Fourier refinement of metaquohemerythrin

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