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Interface characterization of the Type II module pair from fibronectin

Interface characterization of the Type II module pair from fibronectin
Interface characterization of the Type II module pair from fibronectin
The lone 1F22F2 modular pair of fibronectin is found in the collagen-binding region. This exclusive localization suggests the 1F22F2 pair plays an important role in the recognition of collagen. However, no information is currently available about the interaction between the two F2 modules and, thus, the orientation of their putative collagen-binding sites with respect to one another. Comparison of a variety of high-resolution NMR parameters from the F2 modules in isolation and the 1F22F2 pair was used to establish the extent of interaction between the F2 modules in the pair. Chemical shifts of the F2 modules and the 1F22F2 pair indicate that the structures of the modules are preserved in the pair and that, with the exception of the covalent linkage, they do not interact. 15N NMR relaxation data identify significant motion occurring in the linker region of the 1F22F2 pair, and analyses of the anisotropic diffusion properties of the 1F22F2 pair are consistent with the modules in the F2 pair tumbling independent of one another.
8374-8381
Smith, Steven P.
663cd8fd-14b7-4e79-b774-8c7817c2cf42
Hashimoto, Yasuhiro
c0b5dbef-73f6-4d02-a7b4-14e409039c53
Pickford, Andrew R.
a44df69d-1790-43fa-9c04-5d79351e9ab9
Campbell, Iain D.
54eba33e-94f7-450e-b555-c429dc2179de
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Smith, Steven P.
663cd8fd-14b7-4e79-b774-8c7817c2cf42
Hashimoto, Yasuhiro
c0b5dbef-73f6-4d02-a7b4-14e409039c53
Pickford, Andrew R.
a44df69d-1790-43fa-9c04-5d79351e9ab9
Campbell, Iain D.
54eba33e-94f7-450e-b555-c429dc2179de
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115

Smith, Steven P., Hashimoto, Yasuhiro, Pickford, Andrew R., Campbell, Iain D. and Werner, Jörn M. (2000) Interface characterization of the Type II module pair from fibronectin. Biochemistry, 39 (29), 8374-8381. (doi:10.1021/bi000427i).

Record type: Article

Abstract

The lone 1F22F2 modular pair of fibronectin is found in the collagen-binding region. This exclusive localization suggests the 1F22F2 pair plays an important role in the recognition of collagen. However, no information is currently available about the interaction between the two F2 modules and, thus, the orientation of their putative collagen-binding sites with respect to one another. Comparison of a variety of high-resolution NMR parameters from the F2 modules in isolation and the 1F22F2 pair was used to establish the extent of interaction between the F2 modules in the pair. Chemical shifts of the F2 modules and the 1F22F2 pair indicate that the structures of the modules are preserved in the pair and that, with the exception of the covalent linkage, they do not interact. 15N NMR relaxation data identify significant motion occurring in the linker region of the 1F22F2 pair, and analyses of the anisotropic diffusion properties of the 1F22F2 pair are consistent with the modules in the F2 pair tumbling independent of one another.

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More information

e-pub ahead of print date: 30 June 2000
Published date: 25 July 2000
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 372533
URI: http://eprints.soton.ac.uk/id/eprint/372533
PURE UUID: e96044e4-2080-449e-9434-7dde47eda601
ORCID for Jörn M. Werner: ORCID iD orcid.org/0000-0002-4712-1833

Catalogue record

Date deposited: 08 Dec 2014 13:04
Last modified: 15 Mar 2024 03:17

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Contributors

Author: Steven P. Smith
Author: Yasuhiro Hashimoto
Author: Andrew R. Pickford
Author: Iain D. Campbell
Author: Jörn M. Werner ORCID iD

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