FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2105753746> ?p ?o ?g. }

• W2105753746 endingPage "13694" @default.
• W2105753746 startingPage "13687" @default.
• W2105753746 abstract "Aromatic residues in the hydrophobic core of human carbonic anhydrase II (CAII) influence metal ion binding in the active site. Residues F93, F95, and W97 are contained in a beta-strand that also contains two zinc ligands, H94 and H96. The aromatic amino acids contribute to the high zinc affinity and slow zinc dissociation rate constant of CAII [Hunt, J. A., and Fierke, C. A. (1997) J. Biol. Chem. 272, 20364-20372]. Substitution of these aromatic amino acids with smaller side chains enhances Cu(2+) affinity while decreasing Co(2+) and Zn(2+) affinity [Hunt, J. A., Mahiuddin, A., & Fierke, C. A. (1999) Biochemistry 38, 9054-9062]. Here, X-ray crystal structures of zinc-bound F93I/F95M/W97V and F93S/F95L/W97M CAIIs reveal the introduction of new cavities in the hydrophobic core, compensatory movements of surrounding side chains, and the incorporation of buried water molecules; nevertheless, the enzyme maintains tetrahedral zinc coordination geometry. However, a conformational change of direct metal ligand H94 as well as indirect (i.e., second-shell) ligand Q92 accompanies metal release in both F93I/F95M/W97V and F93S/F95L/W97M CAIIs, thereby eliminating preorientation of the histidine ligands with tetrahedral geometry in the apoenzyme. Only one cobalt-bound variant, F93I/F95M/W97V CAII, maintains tetrahedral metal coordination geometry; F93S/F95L/W97M CAII binds Co(2+) with trigonal bipyramidal coordination geometry due to the addition of azide anion to the metal coordination polyhedron. The copper-bound variants exhibit either square pyramidal or trigonal bipyramidal metal coordination geometry due to the addition of a second solvent molecule to the metal coordination polyhedron. The key finding of this work is that aromatic core residues serve as anchors that help to preorient direct and second-shell ligands to optimize zinc binding geometry and destabilize alternative geometries. These geometrical constraints are likely a main determinant of the enhanced zinc/copper specificity of CAII as compared to small molecule chelators." @default.
• W2105753746 created "2016-06-24" @default.
• W2105753746 creator A5015579596 @default.
• W2105753746 creator A5016976113 @default.
• W2105753746 creator A5038614082 @default.
• W2105753746 creator A5058927842 @default.
• W2105753746 creator A5062407037 @default.
• W2105753746 date "2000-10-10" @default.
• W2105753746 modified "2023-09-26" @default.
• W2105753746 title "Structural Influence of Hydrophobic Core Residues on Metal Binding and Specificity in Carbonic Anhydrase II^," @default.
• W2105753746 cites W2016065841 @default.
• W2105753746 cites W2044634803 @default.
• W2105753746 cites W2047514291 @default.
• W2105753746 cites W2070198392 @default.
• W2105753746 cites W2071155271 @default.
• W2105753746 cites W2080476827 @default.
• W2105753746 cites W2106786926 @default.
• W2105753746 cites W4244930290 @default.
• W2105753746 doi "https://doi.org/10.1021/bi001649j" @default.
• W2105753746 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11076507" @default.
• W2105753746 hasPublicationYear "2000" @default.
• W2105753746 type Work @default.
• W2105753746 sameAs 2105753746 @default.
• W2105753746 citedByCount "48" @default.
• W2105753746 countsByYear W21057537462012 @default.
• W2105753746 countsByYear W21057537462013 @default.
• W2105753746 countsByYear W21057537462014 @default.
• W2105753746 countsByYear W21057537462015 @default.
• W2105753746 countsByYear W21057537462016 @default.
• W2105753746 countsByYear W21057537462017 @default.
• W2105753746 countsByYear W21057537462018 @default.
• W2105753746 countsByYear W21057537462019 @default.
• W2105753746 countsByYear W21057537462021 @default.
• W2105753746 countsByYear W21057537462023 @default.
• W2105753746 crossrefType "journal-article" @default.
• W2105753746 hasAuthorship W2105753746A5015579596 @default.
• W2105753746 hasAuthorship W2105753746A5016976113 @default.
• W2105753746 hasAuthorship W2105753746A5038614082 @default.
• W2105753746 hasAuthorship W2105753746A5058927842 @default.
• W2105753746 hasAuthorship W2105753746A5062407037 @default.
• W2105753746 hasConcept C111592845 @default.
• W2105753746 hasConcept C112887158 @default.
• W2105753746 hasConcept C115624301 @default.
• W2105753746 hasConcept C116569031 @default.
• W2105753746 hasConcept C127709339 @default.
• W2105753746 hasConcept C158842870 @default.
• W2105753746 hasConcept C170493617 @default.
• W2105753746 hasConcept C178790620 @default.
• W2105753746 hasConcept C181199279 @default.
• W2105753746 hasConcept C185592680 @default.
• W2105753746 hasConcept C194196696 @default.
• W2105753746 hasConcept C199164860 @default.
• W2105753746 hasConcept C2775914622 @default.
• W2105753746 hasConcept C2778460671 @default.
• W2105753746 hasConcept C2780416268 @default.
• W2105753746 hasConcept C32909587 @default.
• W2105753746 hasConcept C41183919 @default.
• W2105753746 hasConcept C515207424 @default.
• W2105753746 hasConcept C535196362 @default.
• W2105753746 hasConcept C544153396 @default.
• W2105753746 hasConcept C55493867 @default.
• W2105753746 hasConcept C71240020 @default.
• W2105753746 hasConcept C8010536 @default.
• W2105753746 hasConcept C92840921 @default.
• W2105753746 hasConceptScore W2105753746C111592845 @default.
• W2105753746 hasConceptScore W2105753746C112887158 @default.
• W2105753746 hasConceptScore W2105753746C115624301 @default.
• W2105753746 hasConceptScore W2105753746C116569031 @default.
• W2105753746 hasConceptScore W2105753746C127709339 @default.
• W2105753746 hasConceptScore W2105753746C158842870 @default.
• W2105753746 hasConceptScore W2105753746C170493617 @default.
• W2105753746 hasConceptScore W2105753746C178790620 @default.
• W2105753746 hasConceptScore W2105753746C181199279 @default.
• W2105753746 hasConceptScore W2105753746C185592680 @default.
• W2105753746 hasConceptScore W2105753746C194196696 @default.
• W2105753746 hasConceptScore W2105753746C199164860 @default.
• W2105753746 hasConceptScore W2105753746C2775914622 @default.
• W2105753746 hasConceptScore W2105753746C2778460671 @default.
• W2105753746 hasConceptScore W2105753746C2780416268 @default.
• W2105753746 hasConceptScore W2105753746C32909587 @default.
• W2105753746 hasConceptScore W2105753746C41183919 @default.
• W2105753746 hasConceptScore W2105753746C515207424 @default.
• W2105753746 hasConceptScore W2105753746C535196362 @default.
• W2105753746 hasConceptScore W2105753746C544153396 @default.
• W2105753746 hasConceptScore W2105753746C55493867 @default.
• W2105753746 hasConceptScore W2105753746C71240020 @default.
• W2105753746 hasConceptScore W2105753746C8010536 @default.
• W2105753746 hasConceptScore W2105753746C92840921 @default.
• W2105753746 hasIssue "45" @default.
• W2105753746 hasLocation W21057537461 @default.
• W2105753746 hasLocation W21057537462 @default.
• W2105753746 hasOpenAccess W2105753746 @default.
• W2105753746 hasPrimaryLocation W21057537461 @default.
• W2105753746 hasRelatedWork W1994451706 @default.
• W2105753746 hasRelatedWork W2024494343 @default.
• W2105753746 hasRelatedWork W2029737714 @default.
• W2105753746 hasRelatedWork W2052388647 @default.
• W2105753746 hasRelatedWork W2076216380 @default.

• next