Solution structure of a pair of modules from the gelatin-binding domain of fibronectin

A A Bocquier; J R Potts; A R Pickford; I D Campbell

Solution structure of a pair of modules from the gelatin-binding domain of fibronectin

A A Bocquier, J R Potts, A R Pickford, I D Campbell

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

Abstract

Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen.

Original language	English
Pages (from-to)	1451-60
Number of pages	10
Journal	Structure
Volume	7
Issue number	12
Publication status	Published - 1999

Keywords

Amino Acid Sequence
Binding Sites
Collagen
Fibronectins
Gelatin
Humans
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Recombinant Proteins
Solutions

Cite this

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title = "Solution structure of a pair of modules from the gelatin-binding domain of fibronectin",

abstract = "Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen.",

keywords = "Amino Acid Sequence, Binding Sites, Collagen, Fibronectins, Gelatin, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Recombinant Proteins, Solutions",

author = "Bocquier, {A A} and Potts, {J R} and Pickford, {A R} and Campbell, {I D}",

year = "1999",

language = "English",

volume = "7",

pages = "1451--60",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "12",

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TY - JOUR

T1 - Solution structure of a pair of modules from the gelatin-binding domain of fibronectin

AU - Bocquier, A A

AU - Potts, J R

AU - Pickford, A R

AU - Campbell, I D

PY - 1999

Y1 - 1999

N2 - Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen.

AB - Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen.

KW - Amino Acid Sequence

KW - Binding Sites

KW - Collagen

KW - Fibronectins

KW - Gelatin

KW - Humans

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Structure, Secondary

KW - Recombinant Proteins

KW - Solutions

M3 - Article

C2 - 10647176

SN - 0969-2126

VL - 7

SP - 1451

EP - 1460

JO - Structure

JF - Structure

IS - 12

ER -