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Crystal structure of CagL from Helicobacter pylori K74 strain

DC FieldValueLanguage
dc.contributor.author차정헌-
dc.date.accessioned2016-02-04T11:14:49Z-
dc.date.available2016-02-04T11:14:49Z-
dc.date.issued2015-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/139994-
dc.description.abstractHelicobacter pylori (Hp) CagL is a component of the type IV secretion system (T4SS) and interacts with integrin in host cells through its flexible RGD domain to translocate CagA. Differences in CagL amino acid polymorphisms between Western and East-Asian Hps are correlated with clinical outcome. CagL of East-Asian clinical Hp isolate K74 (CagL(K74)) contains multiple residue variations upstream of RGD motif and has different integrin binding affinities compared to those of CagL from Western Hp 26695. Here, we report the crystal structure of CagL(K74). The structure displayed a six-helix bundle including two short α-helices, and the RGD motif was found in the long rigid α2 helix flanked by the conserved protease-sensitive and RGD-helper sequences, as observed in CagL(26695). However, two additional salt bridges were found between the helices compared with the CagL(26695) structure, suggesting that the putative flexible region harboring the RGD motif may be more stable in this CagL variant.-
dc.description.statementOfResponsibilityopen-
dc.relation.isPartOfBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHBacterial Proteins/chemistry*-
dc.subject.MESHBacterial Proteins/metabolism-
dc.subject.MESHCrystallization-
dc.subject.MESHCrystallography, X-Ray-
dc.subject.MESHHelicobacter pylori/chemistry*-
dc.subject.MESHHelicobacter pylori/metabolism-
dc.subject.MESHModels, Molecular-
dc.subject.MESHMolecular Sequence Data-
dc.subject.MESHProtein Binding-
dc.subject.MESHSequence Homology, Amino Acid-
dc.titleCrystal structure of CagL from Helicobacter pylori K74 strain-
dc.typeArticle-
dc.contributor.collegeCollege of Dentistry (치과대학)-
dc.contributor.departmentDept. of Oral Biology (구강생물학)-
dc.contributor.googleauthorJin Myung Choi-
dc.contributor.googleauthorYun Hui Choi-
dc.contributor.googleauthorMuddenahalli Srinivasa Sudhanva-
dc.contributor.googleauthorSundaravinayagam Devakumar-
dc.contributor.googleauthorKun Ho Lee-
dc.contributor.googleauthorJeong-Heon Cha-
dc.contributor.googleauthorSung Haeng Lee-
dc.identifier.doi10.1016/j.bbrc.2015.03.135-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA04007-
dc.contributor.localIdA04144-
dc.relation.journalcodeJ00281-
dc.identifier.eissn1090-2104-
dc.identifier.pmid25839651-
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S0006291X15006014-
dc.subject.keywordCagL-
dc.subject.keywordHelicobacter pylori-
dc.subject.keywordProtein structure-
dc.subject.keywordRGD domain-
dc.subject.keywordT4SS-
dc.contributor.alternativeNameCha, Jung Heon-
dc.contributor.alternativeNameChoi, Yun Hui-
dc.contributor.affiliatedAuthorCha, Jung Heon-
dc.contributor.affiliatedAuthorChoi, Yun Hui-
dc.rights.accessRightsnot free-
dc.citation.volume460-
dc.citation.number4-
dc.citation.startPage964-
dc.citation.endPage970-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol.460(4) : 964-970, 2015-
Appears in Collections:
2. College of Dentistry (치과대학) > Dept. of Oral Biology (구강생물학교실) > 1. Journal Papers

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