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Article: A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein

TitleA cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein
Authors
Issue Date1990
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nature
Citation
Nature, 1990, v. 346 n. 6282, p. 366-369 How to Cite?
AbstractThe gene responsible for cystic fibrosis (CF) has recently been identified and is predicted to encode a protein of 1,480 amino acids called the CF transmembrane conductance regulator (CFTR). Several functional regions are thought to exist in the CFTR protein, including two areas for ATP-binding, termed nucleotide-binding folds (NBFs), a regulatory (R) region that has many possible sites for phosphorylation by protein kinases A and C, and two hydrophobic regions that probably interact with cell membranes. The most common CF gene mutation leads to omission of phenylalanine residue 508 in the putative first NBF, indicating that this region is functionally important. To determine whether other mutations occur in the NBFs of CFTR, we determined the nucleotide sequences of exons 9, 10, 11 and 12 (encoding the first NBF) and exons 20, 21 and 22 (encoding most of the second NBF) from 20 Caucasian and 18 American-black CF patients. One cluster of four mutations was discovered in a 30-base-pair region of exon 11. Three of these mutations cause amino-acid substitutions at residues that are highly conserved among the CFTR protein, the multiple-drug-resistance proteins and ATP-binding membrane-associated transport proteins. The fourth mutation creates a premature termination signal. These mutations reveal a functionally important region in the CFTR protein and provide further evidence that CFTR is a member of the family of ATP-dependent transport proteins.
Persistent Identifierhttp://hdl.handle.net/10722/44238
ISSN
2015 Impact Factor: 38.138
2015 SCImago Journal Rankings: 21.936
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCutting, GRen_HK
dc.contributor.authorKasch, LMen_HK
dc.contributor.authorRosenstein, BJen_HK
dc.contributor.authorZielenski, Jen_HK
dc.contributor.authorTsui, LCen_HK
dc.contributor.authorAntonarakis, SEen_HK
dc.contributor.authorKazazian Jr, HHen_HK
dc.date.accessioned2007-09-12T03:49:38Z-
dc.date.available2007-09-12T03:49:38Z-
dc.date.issued1990en_HK
dc.identifier.citationNature, 1990, v. 346 n. 6282, p. 366-369en_HK
dc.identifier.issn0028-0836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44238-
dc.description.abstractThe gene responsible for cystic fibrosis (CF) has recently been identified and is predicted to encode a protein of 1,480 amino acids called the CF transmembrane conductance regulator (CFTR). Several functional regions are thought to exist in the CFTR protein, including two areas for ATP-binding, termed nucleotide-binding folds (NBFs), a regulatory (R) region that has many possible sites for phosphorylation by protein kinases A and C, and two hydrophobic regions that probably interact with cell membranes. The most common CF gene mutation leads to omission of phenylalanine residue 508 in the putative first NBF, indicating that this region is functionally important. To determine whether other mutations occur in the NBFs of CFTR, we determined the nucleotide sequences of exons 9, 10, 11 and 12 (encoding the first NBF) and exons 20, 21 and 22 (encoding most of the second NBF) from 20 Caucasian and 18 American-black CF patients. One cluster of four mutations was discovered in a 30-base-pair region of exon 11. Three of these mutations cause amino-acid substitutions at residues that are highly conserved among the CFTR protein, the multiple-drug-resistance proteins and ATP-binding membrane-associated transport proteins. The fourth mutation creates a premature termination signal. These mutations reveal a functionally important region in the CFTR protein and provide further evidence that CFTR is a member of the family of ATP-dependent transport proteins.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/natureen_HK
dc.relation.ispartofNatureen_HK
dc.subject.meshAdenosine triphosphate - metabolismen_HK
dc.subject.meshAmino acid sequenceen_HK
dc.subject.meshChromosome mappingen_HK
dc.subject.meshContinental population groupsen_HK
dc.subject.meshMembrane proteins - genetics - metabolismen_HK
dc.titleA cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator proteinen_HK
dc.typeArticleen_HK
dc.identifier.emailTsui, LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui, LC=rp00058en_HK
dc.description.naturelink_to_subscribed_fulltexten_HK
dc.identifier.doi10.1038/346366a0en_HK
dc.identifier.pmid1695717-
dc.identifier.scopuseid_2-s2.0-0025310336en_HK
dc.identifier.volume346en_HK
dc.identifier.issue6282en_HK
dc.identifier.spage366en_HK
dc.identifier.epage369en_HK
dc.identifier.isiWOS:A1990DQ56700062-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridCutting, GR=7006007820en_HK
dc.identifier.scopusauthoridKasch, LM=6603546064en_HK
dc.identifier.scopusauthoridRosenstein, BJ=7102586288en_HK
dc.identifier.scopusauthoridZielenski, J=7003732699en_HK
dc.identifier.scopusauthoridTsui, LC=7102754167en_HK
dc.identifier.scopusauthoridAntonarakis, SE=36049009800en_HK
dc.identifier.scopusauthoridKazazian Jr, HH=7102525271en_HK
dc.identifier.citeulike615813-

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