Hexa‐histidin tag position influences disulfide structure but not binding behavior of in vitro folded N‐terminal domain of rat corticotropin‐releasing factor receptor type 2a
The oxidative folding, particularly the arrangement of disulfide bonds of recombinant extracellular N‐terminal domains of the corticotropin‐releasing factor receptor type 2a bearing five cysteines (C2 to C6), was investigated. Depending on the position of a His‐tag, two types of disulfide patterns w...
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| Veröffentlicht in: | Protein science 2004-09, Vol.13 (9), p.2470-2475 |
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| creator | Klose, Jana Wendt, Norbert Kubald, Sybille Krause, Eberhard Fechner, Klaus Beyermann, Michael Bienert, Michael Rudolph, Rainer Rothemund, Sven |
| description | The oxidative folding, particularly the arrangement of disulfide bonds of recombinant extracellular N‐terminal domains of the corticotropin‐releasing factor receptor type 2a bearing five cysteines (C2 to C6), was investigated. Depending on the position of a His‐tag, two types of disulfide patterns were found. In the case of an N‐terminal His‐tag, the disulfide bonds C2–C3 and C4–C6 were found, leaving C5 free, whereas the C‐terminal position of the His‐tag led to the disulfide pattern C2–C5 and C4–C6, and leaving C3 free. The latter pattern is consistent with the disulfide arrangement of the extracellular N‐terminal domain of the corticotropin‐releasing factor (CRF) receptor type 1, which has six cysteines (C1 to C6) and in which C1 is paired with C3. However, binding data of the two differently disulfide‐bridged domains show no significant differences in binding affinities to selected ligands, indicating the importance of the C‐terminal portion of the N‐terminal receptor domains, particularly the disulfide bond C4–C6 for ligand binding. |
| doi_str_mv | 10.1110/ps.04835904 |
| format | Article |
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Depending on the position of a His‐tag, two types of disulfide patterns were found. In the case of an N‐terminal His‐tag, the disulfide bonds C2–C3 and C4–C6 were found, leaving C5 free, whereas the C‐terminal position of the His‐tag led to the disulfide pattern C2–C5 and C4–C6, and leaving C3 free. The latter pattern is consistent with the disulfide arrangement of the extracellular N‐terminal domain of the corticotropin‐releasing factor (CRF) receptor type 1, which has six cysteines (C1 to C6) and in which C1 is paired with C3. However, binding data of the two differently disulfide‐bridged domains show no significant differences in binding affinities to selected ligands, indicating the importance of the C‐terminal portion of the N‐terminal receptor domains, particularly the disulfide bond C4–C6 for ligand binding.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.04835904</identifier><identifier>PMID: 15295109</identifier><language>eng</language><publisher>Bristol: Cold Spring Harbor Laboratory Press</publisher><subject>ACN, acetonitrile ; Affinity Labels - chemistry ; Affinity Labels - metabolism ; affinity tag ; Amino Acid Sequence ; Animals ; BSA, bovine serum albumin ; CDAP, cyanodimethylaminopyridinium tetrafluoroborate ; Corticotropin-Releasing Hormone - metabolism ; corticotropin‐releasing factor receptor ; CRF, corticotropin‐releasing factor ; Cysteine - chemistry ; Disulfides - chemistry ; DTT, dithiothreitol ; GPCR, G protein–coupled receptor ; GST, glutathione S‐transferase ; GuHCl, guanidinium hydrochloride ; Histidine - chemistry ; Histidine - genetics ; Histidine - metabolism ; HPLC, high‐performance liquid chromatography ; IAA, iodoacetamide ; MALDI, matrix‐assisted laser desorption/ionization ; MBP, maltose binding protein ; Molecular Sequence Data ; MS, mass spectrometry ; NT, N terminus ; Oligopeptides - chemistry ; Oligopeptides - genetics ; Oligopeptides - metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Rats ; Receptors, Corticotropin-Releasing Hormone - chemistry ; Receptors, Corticotropin-Releasing Hormone - genetics ; Receptors, Corticotropin-Releasing Hormone - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; RP, reversed‐phase ; Sequence Alignment ; SPA, scintillation proximity assay ; TOF, time of flight ; Urocortins</subject><ispartof>Protein science, 2004-09, Vol.13 (9), p.2470-2475</ispartof><rights>Copyright © 2004 The Protein Society</rights><rights>Copyright © Copyright 2004 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4200-cbf15a1dc72144467077815c8f19f0b7af811d0de681f178e3ada99020364dc3</citedby><cites>FETCH-LOGICAL-c4200-cbf15a1dc72144467077815c8f19f0b7af811d0de681f178e3ada99020364dc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2280012/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2280012/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15295109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Klose, Jana</creatorcontrib><creatorcontrib>Wendt, Norbert</creatorcontrib><creatorcontrib>Kubald, Sybille</creatorcontrib><creatorcontrib>Krause, Eberhard</creatorcontrib><creatorcontrib>Fechner, Klaus</creatorcontrib><creatorcontrib>Beyermann, Michael</creatorcontrib><creatorcontrib>Bienert, Michael</creatorcontrib><creatorcontrib>Rudolph, Rainer</creatorcontrib><creatorcontrib>Rothemund, Sven</creatorcontrib><title>Hexa‐histidin tag position influences disulfide structure but not binding behavior of in vitro folded N‐terminal domain of rat corticotropin‐releasing factor receptor type 2a</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>The oxidative folding, particularly the arrangement of disulfide bonds of recombinant extracellular N‐terminal domains of the corticotropin‐releasing factor receptor type 2a bearing five cysteines (C2 to C6), was investigated. Depending on the position of a His‐tag, two types of disulfide patterns were found. In the case of an N‐terminal His‐tag, the disulfide bonds C2–C3 and C4–C6 were found, leaving C5 free, whereas the C‐terminal position of the His‐tag led to the disulfide pattern C2–C5 and C4–C6, and leaving C3 free. The latter pattern is consistent with the disulfide arrangement of the extracellular N‐terminal domain of the corticotropin‐releasing factor (CRF) receptor type 1, which has six cysteines (C1 to C6) and in which C1 is paired with C3. However, binding data of the two differently disulfide‐bridged domains show no significant differences in binding affinities to selected ligands, indicating the importance of the C‐terminal portion of the N‐terminal receptor domains, particularly the disulfide bond C4–C6 for ligand binding.</description><subject>ACN, acetonitrile</subject><subject>Affinity Labels - chemistry</subject><subject>Affinity Labels - metabolism</subject><subject>affinity tag</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>BSA, bovine serum albumin</subject><subject>CDAP, cyanodimethylaminopyridinium tetrafluoroborate</subject><subject>Corticotropin-Releasing Hormone - metabolism</subject><subject>corticotropin‐releasing factor receptor</subject><subject>CRF, corticotropin‐releasing factor</subject><subject>Cysteine - chemistry</subject><subject>Disulfides - chemistry</subject><subject>DTT, dithiothreitol</subject><subject>GPCR, G protein–coupled receptor</subject><subject>GST, glutathione S‐transferase</subject><subject>GuHCl, guanidinium hydrochloride</subject><subject>Histidine - chemistry</subject><subject>Histidine - genetics</subject><subject>Histidine - metabolism</subject><subject>HPLC, high‐performance liquid chromatography</subject><subject>IAA, iodoacetamide</subject><subject>MALDI, matrix‐assisted laser desorption/ionization</subject><subject>MBP, maltose binding protein</subject><subject>Molecular Sequence Data</subject><subject>MS, mass spectrometry</subject><subject>NT, N terminus</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - genetics</subject><subject>Oligopeptides - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Rats</subject><subject>Receptors, Corticotropin-Releasing Hormone - chemistry</subject><subject>Receptors, Corticotropin-Releasing Hormone - genetics</subject><subject>Receptors, Corticotropin-Releasing Hormone - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>RP, reversed‐phase</subject><subject>Sequence Alignment</subject><subject>SPA, scintillation proximity assay</subject><subject>TOF, time of flight</subject><subject>Urocortins</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2KFDEQx4Mo7jh68i45eZFeK_2ZvgiyqCssrsgevIV0UpmJdCdtkp51bj6CD-MT-SRmmPHr4qkC9atfFfkT8pjBOWMMns_xHGpeNT3Ud8iK1W1f8L79eJesoG9ZwauWn5EHMX4CgJqV1X1yxpqybxj0K_L9Er_IH1-_bW1MVltHk9zQ2UebrHfUOjMu6BRGqm1cRmM10pjCotISkA5Los4nOliXRzd0wK3cWR-oN3mU7mwKnho_atT0XV6SMEzWyZFqP8kMZCzIRJUPySqf4dm6jAUcUcaD0EiVsi6gwvnwSPsZaSkfkntGjhEfneqa3Lx-dXNxWVxdv3l78fKqUHUJUKjBsEYyrbqS1XXddtB1nDWKG9YbGDppOGMaNLacGdZxrKSWfQ8lVG2tVbUmL47aeRkm1ApdCnIUc7CTDHvhpRX_dpzdio3fibLkAPmn1-TpSRD85wVjEpONCsdROvRLFG3LoWFtn8FnR1AFH2NA83sJA3EIWcxR_Ao500_-vusPe0o1A-URuLUj7v_nEu8_XLOqrDuofgLwbbqO</recordid><startdate>200409</startdate><enddate>200409</enddate><creator>Klose, Jana</creator><creator>Wendt, Norbert</creator><creator>Kubald, Sybille</creator><creator>Krause, Eberhard</creator><creator>Fechner, Klaus</creator><creator>Beyermann, Michael</creator><creator>Bienert, Michael</creator><creator>Rudolph, Rainer</creator><creator>Rothemund, Sven</creator><general>Cold Spring Harbor Laboratory Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200409</creationdate><title>Hexa‐histidin tag position influences disulfide structure but not binding behavior of in vitro folded N‐terminal domain of rat corticotropin‐releasing factor receptor type 2a</title><author>Klose, Jana ; Wendt, Norbert ; Kubald, Sybille ; Krause, Eberhard ; Fechner, Klaus ; Beyermann, Michael ; Bienert, Michael ; Rudolph, Rainer ; Rothemund, Sven</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4200-cbf15a1dc72144467077815c8f19f0b7af811d0de681f178e3ada99020364dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>ACN, acetonitrile</topic><topic>Affinity Labels - chemistry</topic><topic>Affinity Labels - metabolism</topic><topic>affinity tag</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>BSA, bovine serum albumin</topic><topic>CDAP, cyanodimethylaminopyridinium tetrafluoroborate</topic><topic>Corticotropin-Releasing Hormone - metabolism</topic><topic>corticotropin‐releasing factor receptor</topic><topic>CRF, corticotropin‐releasing factor</topic><topic>Cysteine - chemistry</topic><topic>Disulfides - chemistry</topic><topic>DTT, dithiothreitol</topic><topic>GPCR, G protein–coupled receptor</topic><topic>GST, glutathione S‐transferase</topic><topic>GuHCl, guanidinium hydrochloride</topic><topic>Histidine - chemistry</topic><topic>Histidine - genetics</topic><topic>Histidine - metabolism</topic><topic>HPLC, high‐performance liquid chromatography</topic><topic>IAA, iodoacetamide</topic><topic>MALDI, matrix‐assisted laser desorption/ionization</topic><topic>MBP, maltose binding protein</topic><topic>Molecular Sequence Data</topic><topic>MS, mass spectrometry</topic><topic>NT, N terminus</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - genetics</topic><topic>Oligopeptides - metabolism</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Rats</topic><topic>Receptors, Corticotropin-Releasing Hormone - chemistry</topic><topic>Receptors, Corticotropin-Releasing Hormone - genetics</topic><topic>Receptors, Corticotropin-Releasing Hormone - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>RP, reversed‐phase</topic><topic>Sequence Alignment</topic><topic>SPA, scintillation proximity assay</topic><topic>TOF, time of flight</topic><topic>Urocortins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Klose, Jana</creatorcontrib><creatorcontrib>Wendt, Norbert</creatorcontrib><creatorcontrib>Kubald, Sybille</creatorcontrib><creatorcontrib>Krause, Eberhard</creatorcontrib><creatorcontrib>Fechner, Klaus</creatorcontrib><creatorcontrib>Beyermann, Michael</creatorcontrib><creatorcontrib>Bienert, Michael</creatorcontrib><creatorcontrib>Rudolph, Rainer</creatorcontrib><creatorcontrib>Rothemund, Sven</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Klose, Jana</au><au>Wendt, Norbert</au><au>Kubald, Sybille</au><au>Krause, Eberhard</au><au>Fechner, Klaus</au><au>Beyermann, Michael</au><au>Bienert, Michael</au><au>Rudolph, Rainer</au><au>Rothemund, Sven</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hexa‐histidin tag position influences disulfide structure but not binding behavior of in vitro folded N‐terminal domain of rat corticotropin‐releasing factor receptor type 2a</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2004-09</date><risdate>2004</risdate><volume>13</volume><issue>9</issue><spage>2470</spage><epage>2475</epage><pages>2470-2475</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>The oxidative folding, particularly the arrangement of disulfide bonds of recombinant extracellular N‐terminal domains of the corticotropin‐releasing factor receptor type 2a bearing five cysteines (C2 to C6), was investigated. Depending on the position of a His‐tag, two types of disulfide patterns were found. In the case of an N‐terminal His‐tag, the disulfide bonds C2–C3 and C4–C6 were found, leaving C5 free, whereas the C‐terminal position of the His‐tag led to the disulfide pattern C2–C5 and C4–C6, and leaving C3 free. The latter pattern is consistent with the disulfide arrangement of the extracellular N‐terminal domain of the corticotropin‐releasing factor (CRF) receptor type 1, which has six cysteines (C1 to C6) and in which C1 is paired with C3. However, binding data of the two differently disulfide‐bridged domains show no significant differences in binding affinities to selected ligands, indicating the importance of the C‐terminal portion of the N‐terminal receptor domains, particularly the disulfide bond C4–C6 for ligand binding.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>15295109</pmid><doi>10.1110/ps.04835904</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | ACN, acetonitrile Affinity Labels - chemistry Affinity Labels - metabolism affinity tag Amino Acid Sequence Animals BSA, bovine serum albumin CDAP, cyanodimethylaminopyridinium tetrafluoroborate Corticotropin-Releasing Hormone - metabolism corticotropin‐releasing factor receptor CRF, corticotropin‐releasing factor Cysteine - chemistry Disulfides - chemistry DTT, dithiothreitol GPCR, G protein–coupled receptor GST, glutathione S‐transferase GuHCl, guanidinium hydrochloride Histidine - chemistry Histidine - genetics Histidine - metabolism HPLC, high‐performance liquid chromatography IAA, iodoacetamide MALDI, matrix‐assisted laser desorption/ionization MBP, maltose binding protein Molecular Sequence Data MS, mass spectrometry NT, N terminus Oligopeptides - chemistry Oligopeptides - genetics Oligopeptides - metabolism Protein Binding Protein Folding Protein Structure, Tertiary Rats Receptors, Corticotropin-Releasing Hormone - chemistry Receptors, Corticotropin-Releasing Hormone - genetics Receptors, Corticotropin-Releasing Hormone - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RP, reversed‐phase Sequence Alignment SPA, scintillation proximity assay TOF, time of flight Urocortins |
| title | Hexa‐histidin tag position influences disulfide structure but not binding behavior of in vitro folded N‐terminal domain of rat corticotropin‐releasing factor receptor type 2a |
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