Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109.

Singh, Bhanu P; Asthana, Abhishek; Basu, Amrita; Tangirala, Ramakrishna; Mohan Rao, Chintalagiri; Swamy, Musti J

Singh, Bhanu P; Asthana, Abhishek; Basu, Amrita; Tangirala, Ramakrishna; Mohan Rao, Chintalagiri; Swamy, Musti J.

Affiliation

Singh BP; School of Chemistry, University of Hyderabad, India.
Asthana A; Centre for Cellular and Molecular Biology, Hyderabad, India.
Basu A; School of Chemistry, University of Hyderabad, India.
Tangirala R; Centre for Cellular and Molecular Biology, Hyderabad, India.
Mohan Rao C; Centre for Cellular and Molecular Biology, Hyderabad, India.
Swamy MJ; School of Chemistry, University of Hyderabad, India.

FEBS Lett ; 594(3): 509-518, 2020 02.

Article in En | MEDLINE | ID: mdl-31552690

Subject(s)

Cell Membrane/metabolism; Conserved Sequence; Seminal Vesicle Secretory Proteins/chemistry; Seminal Vesicle Secretory Proteins/metabolism; Tryptophan; Amino Acid Sequence; Animals; Cattle; Ligands; Models, Molecular; Mutation; Protein Domains; Protein Multimerization; Protein Structure, Quaternary; Seminal Vesicle Secretory Proteins/genetics

Key words

capacitation; cholesterol efflux; fibronectin type II domain; lipid-protein interaction; molecular chaperone; mutational analysis

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Tryptophan / Cell Membrane / Conserved Sequence / Seminal Vesicle Secretory Proteins Limits: Animals Language: En Journal: FEBS Lett Year: 2020 Document type: Article Affiliation country: India Country of publication: United kingdom

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