FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1521569676> ?p ?o ?g. }

• W1521569676 endingPage "32813" @default.
• W1521569676 startingPage "32807" @default.
• W1521569676 abstract "VILIP and NCS-1, neural-specific, 22-kDa Ca(2+)-binding proteins possessing four EF-hands, were expressed in Escherichia coli to study their divalent cation properties. Flow dialysis (Ca2+ binding) and equilibrium gel filtration (Mg2+ binding) revealed that both recombinant proteins possess only two active metal-binding sites, which can accommodate either Ca2+ or Mg2+. VILIP binds cations without cooperativity with intrinsic affinity constants K'Ca of 1.0 × 10(6) M-1 and K'Mg of 4.8 × 10(3) M-1.Mg2+ antagonizes Ca2+ binding by shifting the isotherms to higher free Ca2+ concentrations without changing their shape. The competition equation yields a K'Mg, comp value of 180 M-1 for both sites. NCS-1 binds two Mg2+ without cooperativity with K'Mg of 8.3 × 10(4) M-1 and two Ca2+ with very strong positive cooperativity (nH = 1.96). In the absence of Mg2+ the K'Ca1 and K'Ca2 values are 8.9 × 10(4) and 1.4 × 10(8) M-1, respectively, which represent an allosteric increase of 1600-fold. Mg2+ shifts the Ca(2+)-binding isotherms to higher Ca2+ concentrations, yielding a K'Mg, comp value of 800 M-1 for both sites. Thus VILIP and NCS-1 show three remarkable differences in the Ca2+/Mg2+ binding parameters: 1) VILIP binds Ca2+ with much lower affinity than NCS-1; 2) VILIP binds Ca2+ in a noncooperative way, whereas NCS-1 shows maximal positive cooperativity; 3) in VILIP the Mg2+/Ca2+ antagonism is much weaker than in NCS-1. Conformational changes monitored by Trp fluorescence indicate that the metal-free forms already are highly structured. Ca2+ binding promotes a 20-30% increase of fluorescence in both proteins, but whereas the Mg2+ form of VILIP has the same fluorescence properties as the metal-free form, Mg(2+)-saturated NCS-1 has those of the Ca2+ form. Near UV difference spectra confirmed that in VILIP the Mg2+ form is very similar to the metal-free form; in NCS-1 it is different, especially in the Tyr region. NCS-1 possesses one unique Cys-38 in EF-hand site I. Its reactivity (kSH) toward 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB) is the same for the Ca(2+)- and Mg(2+)-loaded protein, but kSH is 4-fold higher in metal-free NCS-1. VILIP possesses two additional thiols, one of which is inaccessible to DTNB in the native protein. The reactivity of the two accessible thiols is identical in the metal-free and Mg2+ forms and 5-fold higher than in the Ca2+ form.(ABSTRACT TRUNCATED AT 400 WORDS)" @default.
• W1521569676 created "2016-06-24" @default.
• W1521569676 creator A5002925502 @default.
• W1521569676 creator A5008631938 @default.
• W1521569676 creator A5028223802 @default.
• W1521569676 creator A5029106499 @default.
• W1521569676 creator A5046923893 @default.
• W1521569676 creator A5055723850 @default.
• W1521569676 creator A5057345515 @default.
• W1521569676 date "1994-12-01" @default.
• W1521569676 modified "2023-10-02" @default.
• W1521569676 title "Cation binding and conformational changes in VILIP and NCS-1, two neuron-specific calcium-binding proteins" @default.
• W1521569676 cites W1487909026 @default.
• W1521569676 cites W1504145802 @default.
• W1521569676 cites W1513843435 @default.
• W1521569676 cites W1547929361 @default.
• W1521569676 cites W1558733231 @default.
• W1521569676 cites W1587148368 @default.
• W1521569676 cites W1598970788 @default.
• W1521569676 cites W1641120577 @default.
• W1521569676 cites W1782939187 @default.
• W1521569676 cites W1989295141 @default.
• W1521569676 cites W1989374609 @default.
• W1521569676 cites W1998625959 @default.
• W1521569676 cites W1999354994 @default.
• W1521569676 cites W2008198369 @default.
• W1521569676 cites W2013430098 @default.
• W1521569676 cites W2014000003 @default.
• W1521569676 cites W2014863369 @default.
• W1521569676 cites W2016936460 @default.
• W1521569676 cites W2020295187 @default.
• W1521569676 cites W2021558949 @default.
• W1521569676 cites W2026366752 @default.
• W1521569676 cites W2031403719 @default.
• W1521569676 cites W2033574515 @default.
• W1521569676 cites W2038412379 @default.
• W1521569676 cites W2039366113 @default.
• W1521569676 cites W2042795327 @default.
• W1521569676 cites W2060526583 @default.
• W1521569676 cites W2061734875 @default.
• W1521569676 cites W2068334214 @default.
• W1521569676 cites W2071224136 @default.
• W1521569676 cites W2076298712 @default.
• W1521569676 cites W2078701293 @default.
• W1521569676 cites W2079149343 @default.
• W1521569676 cites W2081722935 @default.
• W1521569676 cites W2088397025 @default.
• W1521569676 cites W2096716204 @default.
• W1521569676 cites W2115201271 @default.
• W1521569676 cites W2120187104 @default.
• W1521569676 cites W2127518311 @default.
• W1521569676 cites W2302602690 @default.
• W1521569676 cites W2403481013 @default.
• W1521569676 cites W2529063792 @default.
• W1521569676 cites W4317926685 @default.
• W1521569676 doi "https://doi.org/10.1016/s0021-9258(20)30063-6" @default.
• W1521569676 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7806504" @default.
• W1521569676 hasPublicationYear "1994" @default.
• W1521569676 type Work @default.
• W1521569676 sameAs 1521569676 @default.
• W1521569676 citedByCount "85" @default.
• W1521569676 countsByYear W15215696762012 @default.
• W1521569676 countsByYear W15215696762013 @default.
• W1521569676 countsByYear W15215696762014 @default.
• W1521569676 countsByYear W15215696762015 @default.
• W1521569676 countsByYear W15215696762018 @default.
• W1521569676 countsByYear W15215696762020 @default.
• W1521569676 countsByYear W15215696762021 @default.
• W1521569676 countsByYear W15215696762022 @default.
• W1521569676 crossrefType "journal-article" @default.
• W1521569676 hasAuthorship W1521569676A5002925502 @default.
• W1521569676 hasAuthorship W1521569676A5008631938 @default.
• W1521569676 hasAuthorship W1521569676A5028223802 @default.
• W1521569676 hasAuthorship W1521569676A5029106499 @default.
• W1521569676 hasAuthorship W1521569676A5046923893 @default.
• W1521569676 hasAuthorship W1521569676A5055723850 @default.
• W1521569676 hasAuthorship W1521569676A5057345515 @default.
• W1521569676 hasBestOaLocation W15215696761 @default.
• W1521569676 hasConcept C122229402 @default.
• W1521569676 hasConcept C12554922 @default.
• W1521569676 hasConcept C169760540 @default.
• W1521569676 hasConcept C178790620 @default.
• W1521569676 hasConcept C185592680 @default.
• W1521569676 hasConcept C2778794669 @default.
• W1521569676 hasConcept C51639874 @default.
• W1521569676 hasConcept C519063684 @default.
• W1521569676 hasConcept C55493867 @default.
• W1521569676 hasConcept C8010536 @default.
• W1521569676 hasConcept C86803240 @default.
• W1521569676 hasConceptScore W1521569676C122229402 @default.
• W1521569676 hasConceptScore W1521569676C12554922 @default.
• W1521569676 hasConceptScore W1521569676C169760540 @default.
• W1521569676 hasConceptScore W1521569676C178790620 @default.
• W1521569676 hasConceptScore W1521569676C185592680 @default.
• W1521569676 hasConceptScore W1521569676C2778794669 @default.
• W1521569676 hasConceptScore W1521569676C51639874 @default.
• W1521569676 hasConceptScore W1521569676C519063684 @default.
• W1521569676 hasConceptScore W1521569676C55493867 @default.

• next