NDLI: The Relationship between Albumin-Binding Capacity of Recombinant Polypeptide and Changes in the Structure of Albumin-Binding Domain

Content Provider	Springer Nature Link
Author	Bormotova, E. A. Gupalova, T. V.
Copyright Year	2015
Abstract	Many bacteria express surface proteins interacting with human serum albumin (HSA). One of these proteins, PAB from anaerobic bacteria, contains an albumin-binding domain consisting of 45 amino acid residues known as GA domain. GA domains are also found in G proteins isolated from human streptococcal strains (groups C and G) and of albumin-binding protein isolated from group G streptococcal strains of animal origin. The GA domain is a left-handed three-helix bundle structure in which amino acid residues of the second and third helixes are involved in albumin binding. We studied the relationship between HSA-binding activity of the recombinant polypeptide isolated from group G streptococcus of animal origin and structure of the GA domain is studied. Structural changes in GA domain significantly attenuated HAS-binding capacity of the recombinant polypeptide. Hence, affinity HSA-binding polypeptide depends on stability of GA domain structure.
Starting Page	393
Ending Page	397
Page Count	5
File Format	PDF
ISSN	00074888
Journal	Bulletin of Experimental Biology and Medicine
Volume Number	159
Issue Number	3
e-ISSN	15738221
Language	English
Publisher	Springer US
Publisher Date	2015-07-25
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	recombinant polypeptide GA domain three-helix bundle structure Biomedicine general Internal Medicine Cell Biology Pathology Laboratory Medicine
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry, Genetics and Molecular Biology

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