The Crystal Structure of CREG, a Secreted Glycoprotein Involved in Cellular Growth and Differentiation
The cellular repressor of E1A-stimulated genes (CREG) is a secreted glycoprotein that inhibits proliferation and enhances differentiation of human embryonal carcinoma cells. CREG binds to the cation-independent mannose 6-phosphate (M6P)/insulin-like growth factor II (IGF2) receptor (IGF2R) (M6P/IGF2...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-12, Vol.102 (51), p.18326-18331 |
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| creator | Sacher, Michael Alessandra Di Bacco Vladimir V. Lunin Zheng Ye Wagner, John Gill, Grace Cygler, Miroslaw Matthews, Brian W. |
| description | The cellular repressor of E1A-stimulated genes (CREG) is a secreted glycoprotein that inhibits proliferation and enhances differentiation of human embryonal carcinoma cells. CREG binds to the cation-independent mannose 6-phosphate (M6P)/insulin-like growth factor II (IGF2) receptor (IGF2R) (M6P/IGF2R), and this receptor has been shown to be required for CREG-induced growth suppression. To better understand CREG function in cellular growth and differentiation, we solved the 3D crystal structure of this protein to 1.9-Å resolution. CREG forms a tight homodimeric complex, and CREG monomers display a β-barrel fold. The three potential glycosylation sites on CREG map to a confined patch opposite the dimer interface. Thus, dimerization of glycosylated CREG likely presents a bivalent ligand for the M6P/IGF2R. Closely related structural homologs of CREG are FMN-binding split-barrel fold proteins that bind flavin mononucleotide. Our structure shows that the putative flavin mononucleotide-binding pocket in CREG is sterically blocked by a loop and several key bulky residues. A mutant of CREG lacking a part of this loop maintained overall structure and dimerization, as well as M6P/IGF2R binding, but lost the growth suppression activity of WT CREG. Thus, analysis of a structure-based mutant of CREG revealed that binding to M6P/IGF2R, while necessary, is not sufficient for CREG-induced growth suppression. These findings indicate that CREG utilizes a known fold for a previously undescribed function. |
| doi_str_mv | 10.1073/pnas.0505071102 |
| format | Article |
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Lunin ; Zheng Ye ; Wagner, John ; Gill, Grace ; Cygler, Miroslaw ; Matthews, Brian W.</creator><creatorcontrib>Sacher, Michael ; Alessandra Di Bacco ; Vladimir V. Lunin ; Zheng Ye ; Wagner, John ; Gill, Grace ; Cygler, Miroslaw ; Matthews, Brian W. ; Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><description>The cellular repressor of E1A-stimulated genes (CREG) is a secreted glycoprotein that inhibits proliferation and enhances differentiation of human embryonal carcinoma cells. CREG binds to the cation-independent mannose 6-phosphate (M6P)/insulin-like growth factor II (IGF2) receptor (IGF2R) (M6P/IGF2R), and this receptor has been shown to be required for CREG-induced growth suppression. To better understand CREG function in cellular growth and differentiation, we solved the 3D crystal structure of this protein to 1.9-Å resolution. CREG forms a tight homodimeric complex, and CREG monomers display a β-barrel fold. The three potential glycosylation sites on CREG map to a confined patch opposite the dimer interface. Thus, dimerization of glycosylated CREG likely presents a bivalent ligand for the M6P/IGF2R. Closely related structural homologs of CREG are FMN-binding split-barrel fold proteins that bind flavin mononucleotide. Our structure shows that the putative flavin mononucleotide-binding pocket in CREG is sterically blocked by a loop and several key bulky residues. A mutant of CREG lacking a part of this loop maintained overall structure and dimerization, as well as M6P/IGF2R binding, but lost the growth suppression activity of WT CREG. Thus, analysis of a structure-based mutant of CREG revealed that binding to M6P/IGF2R, while necessary, is not sufficient for CREG-induced growth suppression. These findings indicate that CREG utilizes a known fold for a previously undescribed function.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0505071102</identifier><identifier>PMID: 16344469</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Animals ; Biochemistry ; Biological Sciences ; CARCINOMAS ; Cell Differentiation ; Cell growth ; Cell Proliferation ; CRYSTAL STRUCTURE ; Crystallography, X-Ray ; Crystals ; DIMERIZATION ; DIMERS ; GENES ; GLYCOPROTEINS ; Glycoproteins - chemistry ; Glycoproteins - genetics ; Glycoproteins - metabolism ; GROWTH FACTORS ; Human growth ; Humans ; MANNOSE ; MATERIALS SCIENCE ; Models, Molecular ; Molecules ; MONOMERS ; MUTANTS ; Mutation - genetics ; national synchrotron light source ; Oxidases ; PROLIFERATION ; Protein Binding ; Protein folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; PROTEINS ; Receptor, IGF Type 2 - metabolism ; Receptors ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; RESIDUES ; RESOLUTION ; Structural Homology, Protein</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-12, Vol.102 (51), p.18326-18331</ispartof><rights>Copyright 2005 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 20, 2005</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c588t-8c5cdcfbb902ca68ea93159c04475203c8359749efb897e2d9dc2477d6e514423</citedby><cites>FETCH-LOGICAL-c588t-8c5cdcfbb902ca68ea93159c04475203c8359749efb897e2d9dc2477d6e514423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/51.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4152616$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4152616$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16344469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/913737$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Sacher, Michael</creatorcontrib><creatorcontrib>Alessandra Di Bacco</creatorcontrib><creatorcontrib>Vladimir V. Lunin</creatorcontrib><creatorcontrib>Zheng Ye</creatorcontrib><creatorcontrib>Wagner, John</creatorcontrib><creatorcontrib>Gill, Grace</creatorcontrib><creatorcontrib>Cygler, Miroslaw</creatorcontrib><creatorcontrib>Matthews, Brian W.</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><title>The Crystal Structure of CREG, a Secreted Glycoprotein Involved in Cellular Growth and Differentiation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The cellular repressor of E1A-stimulated genes (CREG) is a secreted glycoprotein that inhibits proliferation and enhances differentiation of human embryonal carcinoma cells. CREG binds to the cation-independent mannose 6-phosphate (M6P)/insulin-like growth factor II (IGF2) receptor (IGF2R) (M6P/IGF2R), and this receptor has been shown to be required for CREG-induced growth suppression. To better understand CREG function in cellular growth and differentiation, we solved the 3D crystal structure of this protein to 1.9-Å resolution. CREG forms a tight homodimeric complex, and CREG monomers display a β-barrel fold. The three potential glycosylation sites on CREG map to a confined patch opposite the dimer interface. Thus, dimerization of glycosylated CREG likely presents a bivalent ligand for the M6P/IGF2R. Closely related structural homologs of CREG are FMN-binding split-barrel fold proteins that bind flavin mononucleotide. Our structure shows that the putative flavin mononucleotide-binding pocket in CREG is sterically blocked by a loop and several key bulky residues. A mutant of CREG lacking a part of this loop maintained overall structure and dimerization, as well as M6P/IGF2R binding, but lost the growth suppression activity of WT CREG. Thus, analysis of a structure-based mutant of CREG revealed that binding to M6P/IGF2R, while necessary, is not sufficient for CREG-induced growth suppression. These findings indicate that CREG utilizes a known fold for a previously undescribed function.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>CARCINOMAS</subject><subject>Cell Differentiation</subject><subject>Cell growth</subject><subject>Cell Proliferation</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>DIMERIZATION</subject><subject>DIMERS</subject><subject>GENES</subject><subject>GLYCOPROTEINS</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>GROWTH FACTORS</subject><subject>Human growth</subject><subject>Humans</subject><subject>MANNOSE</subject><subject>MATERIALS SCIENCE</subject><subject>Models, Molecular</subject><subject>Molecules</subject><subject>MONOMERS</subject><subject>MUTANTS</subject><subject>Mutation - genetics</subject><subject>national synchrotron light source</subject><subject>Oxidases</subject><subject>PROLIFERATION</subject><subject>Protein Binding</subject><subject>Protein folding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINS</subject><subject>Receptor, IGF Type 2 - metabolism</subject><subject>Receptors</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>RESIDUES</subject><subject>RESOLUTION</subject><subject>Structural Homology, Protein</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdGLEzEQxoMoXq0--yIS70EQ7F2STXaTF-FYz3pwIHjnc0izs3ZLmtQkW-1_b0rLVX2ReUiY_OabyXwIvaTkgpKmutx4ky6IKNFQStgjNKFE0VnNFXmMJoSwZiY542foWUorQogSkjxFZ7SuOOe1mqD-fgm4jbuUjcN3OY42jxFw6HH79Xr-Hht8BzZChg7P3c6GTQwZBo9v_Da4bcmWewvOjc5EPI_hZ15i4zv8ceh7iODzYPIQ_HP0pDcuwYvjOUXfPl3ft59nt1_mN-3V7cwKKfNMWmE72y8WijBraglGVVQoSzhvBCOVlZVQDVfQL6RqgHWqs4w3TVeDoJyzaoo-HHQ342INnS0DROP0Jg5rE3c6mEH__eKHpf4etppWtFFEFYE3B4GQ8qCTHTLYpQ3eg81a0aopMUVvj01i-DFCyno9JFuWYDyEMelaKkrLogt4_g-4CmP0ZQGaEcoUIWI_8uUBsjGkFKF_mJYSvTdZ703WJ5NLxes_P3nij64W4N0R2Fee5JgWVFNZsVr3o3MZfuXC4v-wBXl1QFYph_jAcCpYXXr-BqvxxLk</recordid><startdate>20051220</startdate><enddate>20051220</enddate><creator>Sacher, Michael</creator><creator>Alessandra Di Bacco</creator><creator>Vladimir V. 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Lunin</au><au>Zheng Ye</au><au>Wagner, John</au><au>Gill, Grace</au><au>Cygler, Miroslaw</au><au>Matthews, Brian W.</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Crystal Structure of CREG, a Secreted Glycoprotein Involved in Cellular Growth and Differentiation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-12-20</date><risdate>2005</risdate><volume>102</volume><issue>51</issue><spage>18326</spage><epage>18331</epage><pages>18326-18331</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The cellular repressor of E1A-stimulated genes (CREG) is a secreted glycoprotein that inhibits proliferation and enhances differentiation of human embryonal carcinoma cells. CREG binds to the cation-independent mannose 6-phosphate (M6P)/insulin-like growth factor II (IGF2) receptor (IGF2R) (M6P/IGF2R), and this receptor has been shown to be required for CREG-induced growth suppression. To better understand CREG function in cellular growth and differentiation, we solved the 3D crystal structure of this protein to 1.9-Å resolution. CREG forms a tight homodimeric complex, and CREG monomers display a β-barrel fold. The three potential glycosylation sites on CREG map to a confined patch opposite the dimer interface. Thus, dimerization of glycosylated CREG likely presents a bivalent ligand for the M6P/IGF2R. Closely related structural homologs of CREG are FMN-binding split-barrel fold proteins that bind flavin mononucleotide. Our structure shows that the putative flavin mononucleotide-binding pocket in CREG is sterically blocked by a loop and several key bulky residues. A mutant of CREG lacking a part of this loop maintained overall structure and dimerization, as well as M6P/IGF2R binding, but lost the growth suppression activity of WT CREG. Thus, analysis of a structure-based mutant of CREG revealed that binding to M6P/IGF2R, while necessary, is not sufficient for CREG-induced growth suppression. These findings indicate that CREG utilizes a known fold for a previously undescribed function.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16344469</pmid><doi>10.1073/pnas.0505071102</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Biochemistry Biological Sciences CARCINOMAS Cell Differentiation Cell growth Cell Proliferation CRYSTAL STRUCTURE Crystallography, X-Ray Crystals DIMERIZATION DIMERS GENES GLYCOPROTEINS Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - metabolism GROWTH FACTORS Human growth Humans MANNOSE MATERIALS SCIENCE Models, Molecular Molecules MONOMERS MUTANTS Mutation - genetics national synchrotron light source Oxidases PROLIFERATION Protein Binding Protein folding Protein Structure, Quaternary Protein Structure, Tertiary PROTEINS Receptor, IGF Type 2 - metabolism Receptors Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism RESIDUES RESOLUTION Structural Homology, Protein |
| title | The Crystal Structure of CREG, a Secreted Glycoprotein Involved in Cellular Growth and Differentiation |
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