FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2023341427> ?p ?o ?g. }

• W2023341427 endingPage "496" @default.
• W2023341427 startingPage "485" @default.
• W2023341427 abstract "This is the first crystal structure of a proteolytically generated functional C-lobe of lactoferrin. The purified samples of iron-saturated C-lobe were crystallized in 0.1 M Mes buffer (pH 6.5) containing 25% (v/v) polyethyleneglycol monomethyl ether 550 M and 0.1 M zinc sulphate heptahydrate. The X-ray intensity data were collected with 300 mm imaging plate scanner mounted on a rotating anode generator. The structure was determined by the molecular replacement method using the coordinates of the C-terminal half of bovine lactoferrin as a search model and refined to an R-factor of 0.193 for all data to 1.9A resolution. The final model comprises 2593 protein atoms (residues 342-676 and 681-685), 124 carbohydrate atoms (from ten monosaccharide units, in three glycan chains), one Fe(3+), one CO(3)(2-), two Zn(2+) and 230 water molecules. The overall folding of the C-lobe is essentially the same as that of C-terminal half of bovine lactoferrin but differs slightly in conformations of some of the loops and reveals a number of new interactions. There are 20 Cys residues in the C-lobe forming ten disulphide links. Out of these, one involving Cys481-Cys675 provides an inter-domain link at 2.01A while another Cys405-Cys684 is formed between the main C-lobe 342-676 and the hydrolyzed pentapeptide 681-685 fragment. Six inter-domain hydrogen bonds have been observed in the structure whereas only four were reported in the structure of intact lactoferrin, although domain orientations have been found similar in the two structures. The good quality of electron density has also revealed all the ten oligosaccharide units in the structure. The observation of two metal ions at sites other than the iron-binding cleft is another novel feature of the present structure. These zinc ions stabilize the crystal packing. This structure is also notable for extensive inter-molecular hydrogen bonding in the crystals. Therefore, the present structure appears to be one of the best packed crystal structures among the proteins of the transferrin superfamily." @default.
• W2023341427 created "2016-06-24" @default.
• W2023341427 creator A5003774336 @default.
• W2023341427 creator A5003776760 @default.
• W2023341427 creator A5004808252 @default.
• W2023341427 creator A5005014894 @default.
• W2023341427 date "2003-08-01" @default.
• W2023341427 modified "2023-10-18" @default.
• W2023341427 title "Crystal Structure of a Proteolytically Generated Functional Monoferric C-lobe of Bovine Lactoferrin at 1.9Å Resolution" @default.
• W2023341427 cites W1442483700 @default.
• W2023341427 cites W1512254479 @default.
• W2023341427 cites W1535633114 @default.
• W2023341427 cites W1539796472 @default.
• W2023341427 cites W1546896179 @default.
• W2023341427 cites W1965167915 @default.
• W2023341427 cites W1969559936 @default.
• W2023341427 cites W1971251199 @default.
• W2023341427 cites W1971800897 @default.
• W2023341427 cites W1977914700 @default.
• W2023341427 cites W1980368334 @default.
• W2023341427 cites W1986191025 @default.
• W2023341427 cites W1991431332 @default.
• W2023341427 cites W1993778668 @default.
• W2023341427 cites W1997925804 @default.
• W2023341427 cites W2001641653 @default.
• W2023341427 cites W2004417760 @default.
• W2023341427 cites W2008156329 @default.
• W2023341427 cites W2013083986 @default.
• W2023341427 cites W2014682300 @default.
• W2023341427 cites W2015642465 @default.
• W2023341427 cites W2016900056 @default.
• W2023341427 cites W2028231353 @default.
• W2023341427 cites W2033601613 @default.
• W2023341427 cites W2039772969 @default.
• W2023341427 cites W2046643854 @default.
• W2023341427 cites W2051521963 @default.
• W2023341427 cites W2054163516 @default.
• W2023341427 cites W2056861474 @default.
• W2023341427 cites W2059263441 @default.
• W2023341427 cites W2066634366 @default.
• W2023341427 cites W2072138955 @default.
• W2023341427 cites W2078495582 @default.
• W2023341427 cites W2078748647 @default.
• W2023341427 cites W2088987937 @default.
• W2023341427 cites W2109512555 @default.
• W2023341427 cites W2153994323 @default.
• W2023341427 cites W2282110776 @default.
• W2023341427 cites W4237452153 @default.
• W2023341427 doi "https://doi.org/10.1016/s0022-2836(03)00717-4" @default.
• W2023341427 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12888354" @default.
• W2023341427 hasPublicationYear "2003" @default.
• W2023341427 type Work @default.
• W2023341427 sameAs 2023341427 @default.
• W2023341427 citedByCount "17" @default.
• W2023341427 countsByYear W20233414272012 @default.
• W2023341427 countsByYear W20233414272013 @default.
• W2023341427 countsByYear W20233414272014 @default.
• W2023341427 countsByYear W20233414272016 @default.
• W2023341427 countsByYear W20233414272021 @default.
• W2023341427 crossrefType "journal-article" @default.
• W2023341427 hasAuthorship W2023341427A5003774336 @default.
• W2023341427 hasAuthorship W2023341427A5003776760 @default.
• W2023341427 hasAuthorship W2023341427A5004808252 @default.
• W2023341427 hasAuthorship W2023341427A5005014894 @default.
• W2023341427 hasConcept C108625454 @default.
• W2023341427 hasConcept C115624301 @default.
• W2023341427 hasConcept C185592680 @default.
• W2023341427 hasConcept C206212055 @default.
• W2023341427 hasConcept C2779170986 @default.
• W2023341427 hasConcept C55493867 @default.
• W2023341427 hasConcept C71240020 @default.
• W2023341427 hasConcept C8010536 @default.
• W2023341427 hasConceptScore W2023341427C108625454 @default.
• W2023341427 hasConceptScore W2023341427C115624301 @default.
• W2023341427 hasConceptScore W2023341427C185592680 @default.
• W2023341427 hasConceptScore W2023341427C206212055 @default.
• W2023341427 hasConceptScore W2023341427C2779170986 @default.
• W2023341427 hasConceptScore W2023341427C55493867 @default.
• W2023341427 hasConceptScore W2023341427C71240020 @default.
• W2023341427 hasConceptScore W2023341427C8010536 @default.
• W2023341427 hasIssue "2" @default.
• W2023341427 hasLocation W20233414271 @default.
• W2023341427 hasLocation W20233414272 @default.
• W2023341427 hasOpenAccess W2023341427 @default.
• W2023341427 hasPrimaryLocation W20233414271 @default.
• W2023341427 hasRelatedWork W1974131115 @default.
• W2023341427 hasRelatedWork W2002511335 @default.
• W2023341427 hasRelatedWork W2034550915 @default.
• W2023341427 hasRelatedWork W2080932811 @default.
• W2023341427 hasRelatedWork W2478575474 @default.
• W2023341427 hasRelatedWork W2587011319 @default.
• W2023341427 hasRelatedWork W2606794805 @default.
• W2023341427 hasRelatedWork W2885017315 @default.
• W2023341427 hasRelatedWork W3028214084 @default.
• W2023341427 hasRelatedWork W3158094213 @default.
• W2023341427 hasVolume "331" @default.
• W2023341427 isParatext "false" @default.
• W2023341427 isRetracted "false" @default.

• next