{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T13:48:26Z","timestamp":1780494506267,"version":"3.54.1"},"reference-count":39,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2016,2,24]],"date-time":"2016-02-24T00:00:00Z","timestamp":1456272000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2016,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>The bilobal lactoferrin is an approximately 76 kDa glycoprotein. It sequesters two Fe<jats:sup>3+<\/jats:sup> ions together with two \n<jats:inline-graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"graphic\/prot25004-math-0001.png\" xlink:title=\"urn:x-wiley:08873585:media:prot25004:prot25004-math-0001\"\/> ions. The C\u2010terminal half (residues, Tyr342\u2013Arg689, C\u2010lobe) of bovine lactoferrin (BLF) (residues Ala1\u2013Arg689) was prepared by limited proteolysis using trypsin. Both C\u2010lobe and intact BLF were saturated to 100%. Both of them retained up to nearly 85% of iron at pH 6.5. At pH 5.0, C\u2010lobe retained 75% of iron whereas intact protein could retain only slightly more than 60%. At pH 4.0 both contained 25% iron and at pH 2.0 they were left with iron concentration of only 10%. The structure of iron saturated C\u2010lobe was determined at 2.79 \u00c5 resolution and refined to <jats:italic>R<\/jats:italic><jats:sub>cryst<\/jats:sub> and <jats:italic>R<\/jats:italic><jats:sub>free<\/jats:sub> factors of 0.205 and 0.273, respectively. The structure contains two crystallographically independent molecules, A and B. They were found to have identical structures with an r.m.s. shift of 0.5 \u00c5 for their C<jats:sup>\u03b1<\/jats:sup> atoms. A high solvent content of 66% was observed in the crystals. The average value of an overall B\u2010factor was 68.0 \u00c5<jats:sup>2<\/jats:sup>. The distance of 2.9 \u00c5 observed for the coordination bond between Fe<jats:sup>3+<\/jats:sup> ion and N<jats:sup>e2<\/jats:sup> of His595 appeared to be considerably longer than the normally observed values of 1.9\u20132.2 \u00c5. This indicated that the coordination bond involving His595 may be absent. Other coordination distances were observed in the range of 2.1\u20132.3 \u00c5. Based on the present structure of iron saturated C\u2010lobe, it may be stated that His595 is the first residue to dissociate from ferric ion when the pH is lowered. Proteins 2016; 84:591\u2013599. \u00a9 2016 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/prot.25004","type":"journal-article","created":{"date-parts":[[2016,2,6]],"date-time":"2016-02-06T02:34:25Z","timestamp":1454726065000},"page":"591-599","source":"Crossref","is-referenced-by-count":37,"title":["Structure of iron saturated <scp>C<\/scp>\u2010lobe of bovine lactoferrin at p<scp>H<\/scp> 6.8 indicates a weakening of iron coordination"],"prefix":"10.1002","volume":"84","author":[{"given":"Nilisha","family":"Rastogi","sequence":"first","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Avinash","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prashant K.","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tapesh K.","family":"Tyagi","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sada","family":"Pandey","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kouichirou","family":"Shin","sequence":"additional","affiliation":[{"name":"Functional Food Ingredients Department Morinaga Milk Industry Co. Ltd Kanagawa Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Punit","family":"Kaur","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sujata","family":"Sharma","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tej P.","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,2,24]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1017\/S0022029998003343"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2672.1992.tb05007.x"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.69.3.1469-1476.2001"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2010.05.026"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1136\/adc.67.5.657"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpgi.2001.281.5.G1140"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0090011"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.7.1769"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(89)90602-5"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/18.23.7167"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444999010951"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1997.1386"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1999.2767"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444994013521"},{"key":"e_1_2_7_16_1","first-page":"14","article-title":"Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution","volume":"40","author":"Kumar J","year":"2003","journal-title":"Indian J Biochem Biophys"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1995.0611"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2001.4692"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1107\/S090744490101993X"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998004417"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(89)90283-0"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0108768191008418"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4165(83)90317-3"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1730543"},{"key":"e_1_2_7_25_1","first-page":"575","article-title":"Properties of the iron\u2010binding site of the N\u2010terminal lobe of human and bovine lactotransferrins. Importance of the glycan moiety and of the non\u2010covalent interactions between the N\u2010 and C\u2010terminal lobes in the stability of the iron\u2010binding site","volume":"266","author":"Legrand D","year":"1990","journal-title":"Biochem J"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4838(84)90111-0"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(03)00717-4"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1462"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)49647-6"},{"key":"e_1_2_7_30_1","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1006\/jmbi.1996.0091","article-title":"Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino\u2010terminal half\u2010molecule of human lactoferrin","volume":"256","author":"Faber HR","journal-title":"J Mol Biol"},{"key":"e_1_2_7_31_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444902005127"},{"key":"e_1_2_7_32_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2001.4719"},{"key":"e_1_2_7_33_1","doi-asserted-by":"publisher","DOI":"10.1271\/bbb.60245"},{"key":"e_1_2_7_34_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4615-2548-6_28"},{"key":"e_1_2_7_35_1","doi-asserted-by":"publisher","DOI":"10.1111\/febs.12827"},{"key":"e_1_2_7_36_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(76)90112-4"},{"key":"e_1_2_7_37_1","doi-asserted-by":"publisher","DOI":"10.3168\/jds.S0022-0302(93)77421-4"},{"key":"e_1_2_7_38_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909042589"},{"key":"e_1_2_7_39_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(75)90109-9"},{"key":"e_1_2_7_40_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444911001314"}],"container-title":["Proteins: Structure, Function, and Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.25004","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/prot.25004","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,3]],"date-time":"2023-10-03T14:29:03Z","timestamp":1696343343000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/prot.25004"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,2,24]]},"references-count":39,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2016,5]]}},"alternative-id":["10.1002\/prot.25004"],"URL":"https:\/\/doi.org\/10.1002\/prot.25004","archive":["Portico"],"relation":{},"ISSN":["0887-3585","1097-0134"],"issn-type":[{"value":"0887-3585","type":"print"},{"value":"1097-0134","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,2,24]]}}}