Title : Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I.

Pub. Date : 2005 Jun

PMID : 15907702






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
2 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
3 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
4 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
5 In this work, RA binding to CRABP I is studied in dilute solutions (low micro-molar range), where no dimer and/or oligomer formation occurs. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens