The Atomic Structure of Human Methemalbumin at 1.9 Å

Wardell, Mark R.; Wang, Zhongmin; Ho, Joseph X.; Robert, J Whenham; Rüker, Florian; Ruble, J. R.; Carter, Daniel C.

doi:10.1006/bbrc.2002.6540

Cited by 315 publications

(288 citation statements)

References 30 publications

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“…26,27 These ligands lie in the centre of the four-helix bundle of sub-domain IB, and their interactions with HSA induces significant conformational changes involving side-chain adjustments of sub-domain IB, especially for ligands containing aromatic rings. 12,14,26,27 In addition, this site is exposed to solvent channels in the current crystal form, and thus accessible for in-crystal displacement. However, we observed only some weak electron density at this site that cannot be modeled by a DAUDA molecule, and thus demonstrated no DAUDA in FA1 site.…”

Section: Discussionmentioning

confidence: 99%

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

et al. 2011

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11-(Dansylamino) undecanoic acid (DAUDA) is a dansyl-type fluorophore and has widely used as a probe to determine the binding site for human serum albumin (HSA). Here, we reported that structure of HSA-Myristate-DAUDA ternary complex and identified clearly the presence of two DAUDA molecules at fatty acid (FA) binding site 6 and 7 of HSA, thus showing these two sites are weak FA binding sites. This result also show that DAUDA is an appropriate probe for FA site 6 and 7 on HSA as previous studied, but not a good probe of FA binding site 1 that is likely bilirubin binding site on HSA.

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Section: Discussionmentioning

confidence: 99%

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

et al. 2011

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“…Terminal regions of sequential domains contribute to the formation of interdomain h10-h1 helices linking subdomain IB to subdomain IIA and subdomain IIB to subdomain IIIA, respectively ( Fig. 1) [2,3,[10][11][12][13][14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

“…The FA1 binding site has been shown to be the primary binding site of several ligands, including the heme [14,33]. There is increasing evidence that FA1 has evolved to selectively bind iron(III) heme with high affinity (K d * 10 -8 M) [14-16, 29, 33].…”

Section: Introductionmentioning

confidence: 99%

“…The iron(III) heme propionates protrude from the pocket, pointing toward the interface between domains I and III and are stabilized by salt bridges with His146 and Lys190. A weak coordination between the iron(III) heme and the phenolic oxygen atom of the Tyr161 residue (Fe-O Tyr161 distance 2.73 Å ) was suggested by crystallography [14,33] and further confirmed by resonance Raman spectroscopy [34]. Iron(III) heme is secured to HSA by the long IA-IB connecting loop that fits into the cleft opening [14-16, 29, 33, 34].…”

Section: Introductionmentioning

confidence: 99%

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Evidence for pH-dependent multiple conformers in iron(II) heme–human serum albumin: spectroscopic and kinetic investigation of carbon monoxide binding

et al. 2011

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“…All other parameters were maintained at their default settings. The known crystal structure of HSA (PDB ID:1N5U, Wardell et al, 2002) was obtained from the Brookhaven Protein Data Bank (http://www.rcsb.org/pdb). The structure geometry was optimized using the Tripos force field with a steepest descent method, followed by conjugate gradient in 10 4 steps, and a convergence criterion for the energy gradient of 0.05 KJ/(molÅ).…”

Section: Molecular Dockingmentioning

confidence: 99%

Molecular simulation study of the specific combination between four kinds of phthalic acid esters and human serum albumin

Liang

et al. 2016

Environmental Toxicology and Pharmacology

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a b s t r a c tThe interaction between endocrine disruptor phthalic acid esters (PAEs) and human serum albumin (HSA) was studied by fluorescence spectroscopy and molecular modeling methods. The efficiency of energy transfer and the distance between HSA and PAEs were calculated. The results showed that all of the four kinds of PAEs could quench the intrinsic fluorescence of the HSA, with the mechanisms of static quenching and non-radiative energy transfer. Molecular docking study and thermodynamic analysis revealed that the binding behavior was mainly governed by hydrophobic force. And the results of site marker competitive experiments and modeling method suggested that the four PAEs would mainly bind to the HSA in sub-domain IIIA, which demonstrated that the experimental results could coordinate with the theoretical results. Molecular dynamic simulation (MD) revealed that HSA did have a slight conformational change when it bound with PAEs. It also verified the greater stability of HSA-PAEs complex compared to free protein.

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The Atomic Structure of Human Methemalbumin at 1.9 Å

Cited by 315 publications

References 30 publications

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

A fluorescent fatty acid probe, DAUDA, selectively displaces two myristates bound in human serum albumin

Evidence for pH-dependent multiple conformers in iron(II) heme–human serum albumin: spectroscopic and kinetic investigation of carbon monoxide binding

Molecular simulation study of the specific combination between four kinds of phthalic acid esters and human serum albumin

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