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Article: γ-Crystallin family of the mouse lens: Structural and evolutionary relationships

Titleγ-Crystallin family of the mouse lens: Structural and evolutionary relationships
Authors
Issue Date1984
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 1984, v. 81 n. 24 I, p. 7762-7766 How to Cite?
AbstractThe heterogeneity inherent among γ-crystallins of the mouse lens was investigated by sequence analysis of three γ-crystallin-specific cDNAs. Comparison of the nucleotide sequence of these cDNAs and one previously reported by us revealed that the four γ-cDNAs share 80-90% homology in nucleotide sequence. The entire 3' half of the coding region shows more variability than the 5's half, whereas the greatest variability is observed in the 3' untranslated region where numerous base substitutions, deletions, and insertions seem to have occurred. Alignment of the amino acid sequences of the four mouse γ-crystallins according to the known four structural motifs of the major calf γ-crystallin, γ-II, suggests that all four mouse polypeptides are structurally very similar to calf γ-II. However, most of the mouse polypeptides differ from γ-II by the absence of one amino acid residue, resulting in a shorter connecting peptide between the two globular domains of the protein. Primary sequence alignment also revealed that the four mouse γ-crystallins are most divergent in the third structural motif of the polypeptide. The significance of these differences in terms of the structure and function of the γ-crystallins in the mouse lens is discussed.
Persistent Identifierhttp://hdl.handle.net/10722/44209
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBreitman, MLen_HK
dc.contributor.authorLok, Sen_HK
dc.contributor.authorWistow, Gen_HK
dc.date.accessioned2007-09-12T03:49:03Z-
dc.date.available2007-09-12T03:49:03Z-
dc.date.issued1984en_HK
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 1984, v. 81 n. 24 I, p. 7762-7766en_HK
dc.identifier.issn0027-8424en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44209-
dc.description.abstractThe heterogeneity inherent among γ-crystallins of the mouse lens was investigated by sequence analysis of three γ-crystallin-specific cDNAs. Comparison of the nucleotide sequence of these cDNAs and one previously reported by us revealed that the four γ-cDNAs share 80-90% homology in nucleotide sequence. The entire 3' half of the coding region shows more variability than the 5's half, whereas the greatest variability is observed in the 3' untranslated region where numerous base substitutions, deletions, and insertions seem to have occurred. Alignment of the amino acid sequences of the four mouse γ-crystallins according to the known four structural motifs of the major calf γ-crystallin, γ-II, suggests that all four mouse polypeptides are structurally very similar to calf γ-II. However, most of the mouse polypeptides differ from γ-II by the absence of one amino acid residue, resulting in a shorter connecting peptide between the two globular domains of the protein. Primary sequence alignment also revealed that the four mouse γ-crystallins are most divergent in the third structural motif of the polypeptide. The significance of these differences in terms of the structure and function of the γ-crystallins in the mouse lens is discussed.en_HK
dc.languageengen_HK
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_HK
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshAmino acid sequenceen_HK
dc.subject.meshCrystallins - geneticsen_HK
dc.subject.meshDna - analysisen_HK
dc.subject.meshDna restriction enzymesen_HK
dc.subject.meshLens, crystalline - metabolismen_HK
dc.titleγ-Crystallin family of the mouse lens: Structural and evolutionary relationshipsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0027-8424&volume=81&issue=24&spage=7762&epage=7766&date=1984&atitle=g-crystallin+family+of+the+mouse+lens:+Structural+and+evolutionary+relationshipsen_HK
dc.identifier.emailLok, S: silok@genome.hku.hken_HK
dc.identifier.authorityLok, S=rp00271en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid6096855-
dc.identifier.pmcidPMC392232-
dc.identifier.scopuseid_2-s2.0-0021681827en_HK
dc.identifier.volume81en_HK
dc.identifier.issue24 Ien_HK
dc.identifier.spage7762en_HK
dc.identifier.epage7766en_HK
dc.identifier.isiWOS:A1984AAK5100020-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBreitman, ML=7005448008en_HK
dc.identifier.scopusauthoridLok, S=21035019900en_HK
dc.identifier.scopusauthoridWistow, G=7005967850en_HK

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