Partially structured state of the functional VH domain of the mouse anti-ferritin antibody F11

Abstract

An antibody combining site generally involves the two variable domains, VH from the heavy and VL from the light chain. We expressed the individual VH domain of the mouse anti-human ferritin monoclonal antibody F11. The loss of affinity was not dramatic (K_a=4.0×10⁷ M^-1 versus 8.6×10⁸ M^-1 for the parent antibody) and comparable to that previously observed for other VHs. However, the functional VH domain adopted a partially structured state with a significant amount of distorted secondary and compact yet greatly destabilized tertiary structures, as demonstrated by spectroscopic and calorimetric probes. These data provide the first description for a functional antibody domain that meets all the criteria of a partially structured state.

Original language	English
Pages (from-to)	177-182
Number of pages	6
Journal	FEBS Letters
Volume	518
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)02696-0
Publication status	Published - 8 May 2002
Externally published	Yes

Keywords

Antibody folding and stability
Antigen-binding
VH domain

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(02)02696-0

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Partially structured state of the functional VH domain of the mouse anti-ferritin antibody F11. / Martsev, Sergey P.; Dubnovitsky, Anatoly P.; Stremovsky, Oleg A.; Chumanevich, Alexander A.; Tsybovsky, Yaroslav I.; Kravchuk, Zinaida I.; Deyev, Sergey M.

In: FEBS Letters, Vol. 518, No. 1-3, 08.05.2002, p. 177-182.

Research output: Contribution to journal › Article › peer-review

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title = "Partially structured state of the functional VH domain of the mouse anti-ferritin antibody F11",

abstract = "An antibody combining site generally involves the two variable domains, VH from the heavy and VL from the light chain. We expressed the individual VH domain of the mouse anti-human ferritin monoclonal antibody F11. The loss of affinity was not dramatic (Ka=4.0×107 M-1 versus 8.6×108 M-1 for the parent antibody) and comparable to that previously observed for other VHs. However, the functional VH domain adopted a partially structured state with a significant amount of distorted secondary and compact yet greatly destabilized tertiary structures, as demonstrated by spectroscopic and calorimetric probes. These data provide the first description for a functional antibody domain that meets all the criteria of a partially structured state.",

keywords = "Antibody folding and stability, Antigen-binding, VH domain",

author = "Martsev, {Sergey P.} and Dubnovitsky, {Anatoly P.} and Stremovsky, {Oleg A.} and Chumanevich, {Alexander A.} and Tsybovsky, {Yaroslav I.} and Kravchuk, {Zinaida I.} and Deyev, {Sergey M.}",

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AU - Martsev, Sergey P.

AU - Dubnovitsky, Anatoly P.

AU - Stremovsky, Oleg A.

AU - Chumanevich, Alexander A.

AU - Tsybovsky, Yaroslav I.

AU - Kravchuk, Zinaida I.

AU - Deyev, Sergey M.

PY - 2002/5/8

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AB - An antibody combining site generally involves the two variable domains, VH from the heavy and VL from the light chain. We expressed the individual VH domain of the mouse anti-human ferritin monoclonal antibody F11. The loss of affinity was not dramatic (Ka=4.0×107 M-1 versus 8.6×108 M-1 for the parent antibody) and comparable to that previously observed for other VHs. However, the functional VH domain adopted a partially structured state with a significant amount of distorted secondary and compact yet greatly destabilized tertiary structures, as demonstrated by spectroscopic and calorimetric probes. These data provide the first description for a functional antibody domain that meets all the criteria of a partially structured state.

KW - Antibody folding and stability

KW - Antigen-binding

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