FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2117979814> ?p ?o ?g. }

• W2117979814 endingPage "27258" @default.
• W2117979814 startingPage "27251" @default.
• W2117979814 abstract "Human complement receptor type 2 (CR2 and CD21) is a cell membrane receptor, with 15 or 16 extracellular short consensus repeats (SCRs), that promotes B lymphocyte responses and bridges innate and acquired immunity. The most distally located SCRs, SCR1–2, mediate the interaction of CR2 with its four known ligands (C3d, EBV gp350, IFNα, and CD23). To ascertain specific interacting residues on CR2, we utilized NMR studies wherein gp350 and IFNα were titrated into 15N-labeled SCR1–2, and chemical shift changes indicative of specific inter-molecular interactions were identified. With backbone assignments made, the chemical shift changes were mapped onto the crystal structure of SCR1–2. With regard to gp350, the binding region of CR2 is primarily focused on SCR1 and the inter-SCR linker, specifically residues Asn11, Arg13, Ala22, Arg28, Ser32, Arg36, Lys41, Lys57, Tyr64, Lys67, Tyr68, Arg83, Gly84, and Arg89. With regard to IFNα, the binding is similar to the CR2-C3d interaction with specific residues being Arg13, Tyr16, Arg28, Ser42, Lys48, Lys50, Tyr68, Arg83, Gly84, and Arg89. We also report thermodynamic properties of each ligand-receptor pair determined using isothermal titration calorimetry. The CR2-C3d interaction was characterized as a two-mode binding interaction with Kd values of 0.13 and 160 μm, whereas the CR2-gp350 and CR2-IFNα interactions were characterized as single site binding events with affinities of 0.014 and 0.035 μm, respectively. The compilation of chemical binding maps suggests specific residues on CR2 that are uniquely important in each of these three binding interactions. Human complement receptor type 2 (CR2 and CD21) is a cell membrane receptor, with 15 or 16 extracellular short consensus repeats (SCRs), that promotes B lymphocyte responses and bridges innate and acquired immunity. The most distally located SCRs, SCR1–2, mediate the interaction of CR2 with its four known ligands (C3d, EBV gp350, IFNα, and CD23). To ascertain specific interacting residues on CR2, we utilized NMR studies wherein gp350 and IFNα were titrated into 15N-labeled SCR1–2, and chemical shift changes indicative of specific inter-molecular interactions were identified. With backbone assignments made, the chemical shift changes were mapped onto the crystal structure of SCR1–2. With regard to gp350, the binding region of CR2 is primarily focused on SCR1 and the inter-SCR linker, specifically residues Asn11, Arg13, Ala22, Arg28, Ser32, Arg36, Lys41, Lys57, Tyr64, Lys67, Tyr68, Arg83, Gly84, and Arg89. With regard to IFNα, the binding is similar to the CR2-C3d interaction with specific residues being Arg13, Tyr16, Arg28, Ser42, Lys48, Lys50, Tyr68, Arg83, Gly84, and Arg89. We also report thermodynamic properties of each ligand-receptor pair determined using isothermal titration calorimetry. The CR2-C3d interaction was characterized as a two-mode binding interaction with Kd values of 0.13 and 160 μm, whereas the CR2-gp350 and CR2-IFNα interactions were characterized as single site binding events with affinities of 0.014 and 0.035 μm, respectively. The compilation of chemical binding maps suggests specific residues on CR2 that are uniquely important in each of these three binding interactions." @default.
• W2117979814 created "2016-06-24" @default.
• W2117979814 creator A5020468097 @default.
• W2117979814 creator A5040063597 @default.
• W2117979814 creator A5066321625 @default.
• W2117979814 creator A5088895093 @default.
• W2117979814 date "2010-08-01" @default.
• W2117979814 modified "2023-09-27" @default.
• W2117979814 title "Biophysical Investigations of Complement Receptor 2 (CD21 and CR2)-Ligand Interactions Reveal Amino Acid Contacts Unique to Each Receptor-Ligand Pair" @default.
• W2117979814 cites W1499309587 @default.
• W2117979814 cites W1518090161 @default.
• W2117979814 cites W1536557099 @default.
• W2117979814 cites W1556075436 @default.
• W2117979814 cites W1571303653 @default.
• W2117979814 cites W1578564117 @default.
• W2117979814 cites W1579336178 @default.
• W2117979814 cites W1585469912 @default.
• W2117979814 cites W1587809300 @default.
• W2117979814 cites W1599196825 @default.
• W2117979814 cites W1604303666 @default.
• W2117979814 cites W1604837267 @default.
• W2117979814 cites W1642607010 @default.
• W2117979814 cites W1670033943 @default.
• W2117979814 cites W1859617576 @default.
• W2117979814 cites W1910430498 @default.
• W2117979814 cites W1923905700 @default.
• W2117979814 cites W1938707196 @default.
• W2117979814 cites W1956759320 @default.
• W2117979814 cites W1966133239 @default.
• W2117979814 cites W1967738350 @default.
• W2117979814 cites W1972624990 @default.
• W2117979814 cites W1973640489 @default.
• W2117979814 cites W1983556802 @default.
• W2117979814 cites W1988712577 @default.
• W2117979814 cites W1993659659 @default.
• W2117979814 cites W2002561725 @default.
• W2117979814 cites W2003458079 @default.
• W2117979814 cites W2010819361 @default.
• W2117979814 cites W2011216554 @default.
• W2117979814 cites W2016899230 @default.
• W2117979814 cites W2019592934 @default.
• W2117979814 cites W2020357919 @default.
• W2117979814 cites W2022496873 @default.
• W2117979814 cites W2038129036 @default.
• W2117979814 cites W2042498963 @default.
• W2117979814 cites W2047193748 @default.
• W2117979814 cites W2063160610 @default.
• W2117979814 cites W2074753043 @default.
• W2117979814 cites W2076074155 @default.
• W2117979814 cites W2078225503 @default.
• W2117979814 cites W2100740815 @default.
• W2117979814 cites W2106273198 @default.
• W2117979814 cites W2110658123 @default.
• W2117979814 cites W2112249032 @default.
• W2117979814 cites W2112543526 @default.
• W2117979814 cites W2127373373 @default.
• W2117979814 cites W2128585134 @default.
• W2117979814 cites W2139316669 @default.
• W2117979814 cites W2142149565 @default.
• W2117979814 cites W2144361076 @default.
• W2117979814 cites W2147281292 @default.
• W2117979814 cites W2153983456 @default.
• W2117979814 cites W2164998591 @default.
• W2117979814 cites W2169697968 @default.
• W2117979814 cites W2169707043 @default.
• W2117979814 cites W2169821755 @default.
• W2117979814 cites W2170398666 @default.
• W2117979814 doi "https://doi.org/10.1074/jbc.m110.106617" @default.
• W2117979814 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2930724" @default.
• W2117979814 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20558730" @default.
• W2117979814 hasPublicationYear "2010" @default.
• W2117979814 type Work @default.
• W2117979814 sameAs 2117979814 @default.
• W2117979814 citedByCount "10" @default.
• W2117979814 countsByYear W21179798142013 @default.
• W2117979814 countsByYear W21179798142017 @default.
• W2117979814 countsByYear W21179798142021 @default.
• W2117979814 countsByYear W21179798142023 @default.
• W2117979814 crossrefType "journal-article" @default.
• W2117979814 hasAuthorship W2117979814A5020468097 @default.
• W2117979814 hasAuthorship W2117979814A5040063597 @default.
• W2117979814 hasAuthorship W2117979814A5066321625 @default.
• W2117979814 hasAuthorship W2117979814A5088895093 @default.
• W2117979814 hasBestOaLocation W21179798141 @default.
• W2117979814 hasConcept C107824862 @default.
• W2117979814 hasConcept C111684460 @default.
• W2117979814 hasConcept C116569031 @default.
• W2117979814 hasConcept C12554922 @default.
• W2117979814 hasConcept C156911925 @default.
• W2117979814 hasConcept C159654299 @default.
• W2117979814 hasConcept C170493617 @default.
• W2117979814 hasConcept C175773311 @default.
• W2117979814 hasConcept C185592680 @default.
• W2117979814 hasConcept C187250156 @default.
• W2117979814 hasConcept C51639874 @default.
• W2117979814 hasConcept C54355233 @default.
• W2117979814 hasConcept C55493867 @default.
• W2117979814 hasConcept C71240020 @default.

• next