Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin
Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution s...
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| Veröffentlicht in: | Journal of biomolecular NMR 2007-04, Vol.37 (4), p.321-328 |
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| container_title | Journal of biomolecular NMR |
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| creator | Wolf, Christian A Dancea, Felician Shi, Meichen Bade-Noskova, Veronika Rüterjans, Heinz Kerjaschki, Dontscho Lücke, Christian |
| description | Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short β-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence. |
| doi_str_mv | 10.1007/s10858-006-9129-3 |
| format | Article |
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Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short β-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.</description><identifier>ISSN: 0925-2738</identifier><identifier>EISSN: 1573-5001</identifier><identifier>DOI: 10.1007/s10858-006-9129-3</identifier><identifier>PMID: 17245526</identifier><language>eng</language><publisher>Netherlands: Dordrecht : Kluwer Academic Publishers</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Calcium - chemistry ; Calcium cage ; Cysteine - chemistry ; Cysteine-rich repeat ; LDLR gene family ; Ligand-binding domain ; Ligands ; Low density lipoprotein receptor ; Low Density Lipoprotein Receptor-Related Protein-2 - chemistry ; Low density lipoprotein receptors ; Molecular Sequence Data ; Protein Folding ; Protein Structure, Secondary ; Proteins ; Rats ; Repetitive Sequences, Nucleic Acid ; Rodents ; Solutions - chemistry ; Static Electricity</subject><ispartof>Journal of biomolecular NMR, 2007-04, Vol.37 (4), p.321-328</ispartof><rights>Springer Science+Business Media B.V. 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c350t-ac1a7de4a0ca90490a41e16c47a7e4a3f2bb1d6bbe188d53bb03256471f1f1473</citedby><cites>FETCH-LOGICAL-c350t-ac1a7de4a0ca90490a41e16c47a7e4a3f2bb1d6bbe188d53bb03256471f1f1473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17245526$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wolf, Christian A</creatorcontrib><creatorcontrib>Dancea, Felician</creatorcontrib><creatorcontrib>Shi, Meichen</creatorcontrib><creatorcontrib>Bade-Noskova, Veronika</creatorcontrib><creatorcontrib>Rüterjans, Heinz</creatorcontrib><creatorcontrib>Kerjaschki, Dontscho</creatorcontrib><creatorcontrib>Lücke, Christian</creatorcontrib><title>Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin</title><title>Journal of biomolecular NMR</title><addtitle>J Biomol NMR</addtitle><description>Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short β-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Calcium - chemistry</subject><subject>Calcium cage</subject><subject>Cysteine - chemistry</subject><subject>Cysteine-rich repeat</subject><subject>LDLR gene family</subject><subject>Ligand-binding domain</subject><subject>Ligands</subject><subject>Low density lipoprotein receptor</subject><subject>Low Density Lipoprotein Receptor-Related Protein-2 - chemistry</subject><subject>Low density lipoprotein receptors</subject><subject>Molecular Sequence Data</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Rats</subject><subject>Repetitive Sequences, Nucleic Acid</subject><subject>Rodents</subject><subject>Solutions - 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chemistry</topic><topic>Calcium cage</topic><topic>Cysteine - chemistry</topic><topic>Cysteine-rich repeat</topic><topic>LDLR gene family</topic><topic>Ligand-binding domain</topic><topic>Ligands</topic><topic>Low density lipoprotein receptor</topic><topic>Low Density Lipoprotein Receptor-Related Protein-2 - chemistry</topic><topic>Low density lipoprotein receptors</topic><topic>Molecular Sequence Data</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Rats</topic><topic>Repetitive Sequences, Nucleic Acid</topic><topic>Rodents</topic><topic>Solutions - chemistry</topic><topic>Static Electricity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wolf, Christian A</creatorcontrib><creatorcontrib>Dancea, Felician</creatorcontrib><creatorcontrib>Shi, Meichen</creatorcontrib><creatorcontrib>Bade-Noskova, Veronika</creatorcontrib><creatorcontrib>Rüterjans, Heinz</creatorcontrib><creatorcontrib>Kerjaschki, Dontscho</creatorcontrib><creatorcontrib>Lücke, Christian</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - 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Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short β-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.</abstract><cop>Netherlands</cop><pub>Dordrecht : Kluwer Academic Publishers</pub><pmid>17245526</pmid><doi>10.1007/s10858-006-9129-3</doi><tpages>8</tpages></addata></record> |
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| issn | 0925-2738 1573-5001 |
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| source | MEDLINE; Springer Online Journals Complete |
| subjects | Amino Acid Motifs Amino Acid Sequence Animals Calcium - chemistry Calcium cage Cysteine - chemistry Cysteine-rich repeat LDLR gene family Ligand-binding domain Ligands Low density lipoprotein receptor Low Density Lipoprotein Receptor-Related Protein-2 - chemistry Low density lipoprotein receptors Molecular Sequence Data Protein Folding Protein Structure, Secondary Proteins Rats Repetitive Sequences, Nucleic Acid Rodents Solutions - chemistry Static Electricity |
| title | Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin |
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