Docking of calcium ions in proteins with flexible side chains and deformable backbones (Q57130626)

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Language	Label	Description	Also known as
English	Docking of calcium ions in proteins with flexible side chains and deformable backbones	No description defined

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scholarly article

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Docking of calcium ions in proteins with flexible side chains and deformable backbones (English)

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author name string

Ricky C K Cheng

1

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Boris S Zhorov

2

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language of work or name

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publication date

April 2010

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European Biophysics Journal

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39

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5

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825-38

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Predicting calcium-binding sites in proteins - a graph theory and geometry approach.

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Monte Carlo-minimized energy profile of estradiol in the ligand-binding tunnel of 17 beta-hydroxysteroid dehydrogenase: atomic mechanisms of steroid recognition

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Prediction of water and metal binding sites and their affinities by using the Fold-X force field

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A united residue force-field for calcium-protein interactions.

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Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c

1 reference

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The Protein Data Bank

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Structural analysis, identification, and design of calcium-binding sites in proteins

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Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y

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Divalent cations modulate the activity of metabotropic glutamate receptors

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Structural characteristics of protein binding sites for calcium and lanthanide ions

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Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

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Characterizing the microenvironment surrounding protein sites

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Calcium-binding sites in proteins: a structural perspective

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Where metal ions bind in proteins

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Free-energy linkage between folding and calcium binding in EF-hand proteins

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Predicting metal-binding site residues in low-resolution structural models.

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Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium

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Structure of native porcine pancreatic elastase at 1.65 A resolutions

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Identification and dissection of Ca(2+)-binding sites in the extracellular domain of Ca(2+)-sensing receptor

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Calcium signaling

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Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

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Effective energy function for proteins in solution

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Sodium channels: ionic model of slow inactivation and state-dependent drug binding

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Structural and energetic parameters of Ca2+ binding to peptides and proteins

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Monte Carlo-energy minimization of correolide in the Kv1.3 channel: possible role of potassium ion in ligand-receptor interactions

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The enzymatic activity of proteinase K is controlled by calcium.

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Recognizing protein binding sites using statistical descriptions of their 3D environments

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Rational design of a calcium-binding protein

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Are predicted structures good enough to preserve functional sites?

1 reference

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Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein

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Calmodulin structure refined at 1.7 A resolution

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Calcium-dependent stability studies of domains 1 and 2 of epithelial cadherin

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Small revisions to predicted distances around metal sites in proteins

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Molecular modeling of benzothiazepine binding in the L-type calcium channel

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Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features

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Synchrotron X-ray data collection and restrained least-squares refinement of the crystal structure of proteinase K at 1.5 A resolution

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ROSETTALIGAND: protein-small molecule docking with full side-chain flexibility

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Conservative D133E mutation of calmodulin site IV drastically alters calcium binding and phosphodiesterase regulation.

1 reference

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Homology model of dihydropyridine receptor: implications for L-type Ca(2+) channel modulation by agonists and antagonists

1 reference

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A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases

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1 reference

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Monte Carlo-minimization approach to the multiple-minima problem in protein folding

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Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis

1 reference

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10.1007/S00249-009-0561-7

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