CD151 a membrane protein via X-ray crystallography

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dc.contributor.author Purushothaman, Gayathri
dc.contributor.author Thiruvenkatam, Vijay
dc.date.accessioned 2018-01-08T12:33:52Z
dc.date.available 2018-01-08T12:33:52Z
dc.date.issued 2017-08
dc.identifier.citation Purushothaman, Gayathri and Thiruvenkatam, Vijay, "CD151 a membrane protein via X-ray crystallography", Acta Crystallographica Section A, DOI: 10.1107/S205327331709180X, vol. 73, no. a2, pp. C393, Aug. 2017. (Abstract) en_US
dc.identifier.issn 2053-2733
dc.identifier.uri http://dx.doi.org/10.1107/S205327331709180X
dc.identifier.uri http://repository.iitgn.ac.in/handle/123456789/3379
dc.description.abstract Tetraspanins are family of small membrane proteins and they are involved in multitude of biological process. Structurally theyare characterized by having four transmembrane domains, short inner and outer loops, one large extra cellular loop containsCCG motif and N and C terminal. Iconic features of these proteins are formation of Tetraspanin Enriched Micro domains(TEMs) by interacting among themselves and with other transmembrane and cytosolic proteins. These domains provide asignaling platform for many important cellular functions such as immune response induction, fertilization, viral infection,maintenance of skin integrity and malignant process. Tetraspanin CD151 is frequently over expressed on cancer cells and isfunctionally linked to cancer metastasis. CD151 forms direct and stable and interaction with integrin molecules and regulatesthe cellular functions. Increasing evidence emerging from in vitro, in vivo and clinical analyses associates that CD151partnership with integrins ?6?1 and ?6?4, modulates different stages in cancer such as tumor cell growth, metastasis anddrug sensitivity in various types of cancer. The importance of CD151 signposts that targeting CD151 could be a promisingtherapy in cancer and other viral infections. Even though evidences are there for the CD151-Integrin interactions, themechanisms and mode of the interactions are not yet known. The structural and functional characteristics of CD151 via thethree dimensional structure of the protein would pave way for understanding the TEMs of CD151. By considering thechallenges in the structural determination of membrane protein, we expressed and purified the specific portion of CD151 inbacterial system. The expressed portion includes large extra cellular loop alone as well along with the one transmembranedomain and C-Terminal which expected to be have interaction with Integrins and other partner proteins. The expressedrecombinant protein confirmed by western blot and MALDI. The activity of the recombinant protein will be assessed bycholesterol binding assays followed the protein will be experiment to crystallization.
dc.description.statementofresponsibility by Gayathri Purushothaman and Vijay Thiruvenkatam
dc.format.extent vol. 73, no. a2, pp. C393
dc.language.iso en en_US
dc.publisher International Union of Crystallography en_US
dc.subject Tetraspanin en_US
dc.subject CD151 en_US
dc.subject 3D Structure en_US
dc.title CD151 a membrane protein via X-ray crystallography en_US
dc.type Article en_US
dc.relation.journal Acta Crystallographica Section A


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