(Q78169813)

English

Investigation of the binding interactions of progesterone using muteins of the human progesterone receptor ligand binding domain designed on the basis of a three-dimensional protein model

scientific article published on 01 January 1999

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scholarly article

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12 December 2019

Investigation of the binding interactions of progesterone using muteins of the human progesterone receptor ligand binding domain designed on the basis of a three-dimensional protein model (English)

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12 December 2019

Jean-Marie Wurtz

7

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12 December 2019

author name string

M Letz

1

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12 December 2019

P Bringmann

2

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12 December 2019

M Mann

3

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12 December 2019

A Mueller-Fahrnow

4

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12 December 2019

D Reipert

5

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12 December 2019

P Scholz

6

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12 December 2019

U Egner

8

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12 December 2019

language of work or name

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publication date

1 January 1999

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12 December 2019

number of pages

10

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Biochimica et Biophysica Acta

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12 December 2019

1429

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12 December 2019

2

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12 December 2019

391-400

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12 December 2019

The nuclear receptor ligand-binding domain: structure and function.

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Molecular mechanisms of action of steroid/thyroid receptor superfamily members

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The nuclear receptor superfamily: the second decade

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid

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A structural role for hormone in the thyroid hormone receptor.

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Molecular basis of agonism and antagonism in the oestrogen receptor

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The Protein Data Bank. A computer-based archival file for macromolecular structures

1 reference

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Induction of a novel conformation in the progesterone receptor by ZK299 involves a defined region of the carboxyl-terminal tail

1 reference

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7 January 2021

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A single amino acid that determines the sensitivity of progesterone receptors to RU486.

1 reference

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7 January 2021

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Point Mutation in the Ligand-Binding Domain of the Progesterone Receptor Generates a Transdominant Negative Phenotype

1 reference

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7 January 2021

based on heuristic

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The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor

1 reference

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7 January 2021

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Switching agonistic, antagonistic, and mixed transcriptional responses to 11 beta-substituted progestins by mutation of the progesterone receptor

1 reference

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7 January 2021

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Atomic structure of progesterone complexed with its receptor

1 reference

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

1 reference

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Three-dimensional models of estrogen receptor ligand binding domain complexes, based on related crystal structures and mutational and structure-activity relationship data.

1 reference

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7 January 2021

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

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7 January 2021

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Amino acid similarity coefficients for protein modeling and sequence alignment derived from main-chain folding angles

1 reference

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Suggestions for "safe" residue substitutions in site-directed mutagenesis.

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Altered ligand binding properties and enhanced stability of a constitutively active estrogen receptor: evidence that an open pocket conformation is required for ligand interaction.

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7 January 2021

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Cysteines 638 and 665 in the hormone binding domain of human glucocorticoid receptor define the specificity to glucocorticoids

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7 January 2021

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Antagonism in the human mineralocorticoid receptor.

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7 January 2021

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ALSCRIPT: a tool to format multiple sequence alignments

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Identifiers

10.1016/S0167-4838(98)00249-0

1 reference

Europe PubMed Central

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12 December 2019

1 reference

Europe PubMed Central

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12 December 2019

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