Flexibility and extracellular opening determine the interaction between ligands and insect sulfakinin receptors.

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Flexibility and extracellular opening determine the interaction between ligands and insect sulfakinin receptors.

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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Flexibility and extracellular ...... d insect sulfakinin receptors.

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Flexibility and extracellular ...... d insect sulfakinin receptors.

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Flexibility and extracellular ...... d insect sulfakinin receptors.

@en

Flexibility and extracellular ...... d insect sulfakinin receptors.

@nl

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Flexibility and extracellular ...... d insect sulfakinin receptors.

@en

Flexibility and extracellular ...... d insect sulfakinin receptors.

@nl

P1476

Flexibility and extracellular ...... d insect sulfakinin receptors.

@en

P2093

Antônio S K Braz

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Freja Scheys

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Moises João Zotti

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Na Yu

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Pedro H C Penna

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P2860

Arginine 197 of the cholecystokinin-A receptor binding site interacts with the sulfate of the peptide agonist cholecystokinin

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

Evidence for a direct interaction between the penultimate aspartic acid of cholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptor

A segment of five amino acids in the second extracellular loop of the cholecystokinin-B receptor is essential for selectivity of the peptide agonist gastrin

GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit.

Conformer generation with OMEGA: algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database.

Screening of antifeedant activity in brain extracts led to the identification of sulfakinin as a satiety promoter in the German cockroach. Are arthropod sulfakinins homologous to vertebrate gastrins-cholecystokinins?

CHARMM-GUI Membrane Builder toward realistic biological membrane simulations.

Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin.

Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state.

P2888

srep12627

P304

12627

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scholarly article

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10.1038/SREP12627

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English

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P50

Guy Smagghe

Ronald J Nachman

P577

2015-08-12T00:00:00Z

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P5875

280937194

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P6179

1037378141

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26267367

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4542541

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