Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls

Janet E. Lovett; Rachel J. M. Abbott; Pietro Roversi; Steven Johnson; Joseph J. E. Caesar; Marianna Doria; Gunnar Jeschke; Christiane R. Timmel; Susan M. Lea

doi:10.1080/00268976.2013.827754

Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls

Janet E. Lovett^*, Rachel J. M. Abbott, Pietro Roversi, Steven Johnson, Joseph J. E. Caesar, Marianna Doria, Gunnar Jeschke, Christiane R. Timmel, Susan M. Lea

^*Corresponding author for this work

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

Abstract

The electron paramagnetic resonance technique of double electron-electron resonance (DEER) was used to measure nanometre-scale distances between nitroxide spin labels attached to the complement regulatory protein CD55 (also known as decay accelerating factor) and the von Willebrand factor A (vWF-A) domain of factor B. Following a thorough assessment of the quality of the data, distances obtained from good-quality measurements are compared to predicted distances from a previously hypothesised model for the complex and are found to be incompatible. The success of using these distances as restraints in multi-body docking routines is presented critically.

Original language	English
Pages (from-to)	2865-2872
Number of pages	8
Journal	Molecular Physics
Volume	111
Issue number	18-19
DOIs	https://doi.org/10.1080/00268976.2013.827754
Publication status	Published - 1 Oct 2013

Keywords

DEER
distance restraints
CD55
vWF-A
decay acceleration
DECAY-ACCELERATING FACTOR
PATHWAY C3 CONVERTASE
DISTANCE MEASUREMENTS
ALTERNATIVE PATHWAY
ESCHERICHIA-COLI
EPR SPECTROSCOPY
NMR SYSTEM
REFINEMENT
MODEL
BIOMACROMOLECULES

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10.1080/00268976.2013.827754

Royal Society Research Fellowship: Royal Society Research Fellowship
Lovett, J. E. (PI)
The Royal Society
1/05/14 → 15/02/17
Project: Fellowship

Cite this

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title = "Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls",

abstract = "The electron paramagnetic resonance technique of double electron-electron resonance (DEER) was used to measure nanometre-scale distances between nitroxide spin labels attached to the complement regulatory protein CD55 (also known as decay accelerating factor) and the von Willebrand factor A (vWF-A) domain of factor B. Following a thorough assessment of the quality of the data, distances obtained from good-quality measurements are compared to predicted distances from a previously hypothesised model for the complex and are found to be incompatible. The success of using these distances as restraints in multi-body docking routines is presented critically.",

keywords = "DEER, distance restraints, CD55, vWF-A, decay acceleration, DECAY-ACCELERATING FACTOR, PATHWAY C3 CONVERTASE, DISTANCE MEASUREMENTS, ALTERNATIVE PATHWAY, ESCHERICHIA-COLI, EPR SPECTROSCOPY, NMR SYSTEM, REFINEMENT, MODEL, BIOMACROMOLECULES",

author = "Lovett, {Janet E.} and Abbott, {Rachel J. M.} and Pietro Roversi and Steven Johnson and Caesar, {Joseph J. E.} and Marianna Doria and Gunnar Jeschke and Timmel, {Christiane R.} and Lea, {Susan M.}",

year = "2013",

month = oct,

day = "1",

doi = "10.1080/00268976.2013.827754",

language = "English",

volume = "111",

pages = "2865--2872",

journal = "Molecular Physics",

issn = "0026-8976",

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TY - JOUR

T1 - Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls

AU - Lovett, Janet E.

AU - Abbott, Rachel J. M.

AU - Roversi, Pietro

AU - Johnson, Steven

AU - Caesar, Joseph J. E.

AU - Doria, Marianna

AU - Jeschke, Gunnar

AU - Timmel, Christiane R.

AU - Lea, Susan M.

PY - 2013/10/1

Y1 - 2013/10/1

N2 - The electron paramagnetic resonance technique of double electron-electron resonance (DEER) was used to measure nanometre-scale distances between nitroxide spin labels attached to the complement regulatory protein CD55 (also known as decay accelerating factor) and the von Willebrand factor A (vWF-A) domain of factor B. Following a thorough assessment of the quality of the data, distances obtained from good-quality measurements are compared to predicted distances from a previously hypothesised model for the complex and are found to be incompatible. The success of using these distances as restraints in multi-body docking routines is presented critically.

AB - The electron paramagnetic resonance technique of double electron-electron resonance (DEER) was used to measure nanometre-scale distances between nitroxide spin labels attached to the complement regulatory protein CD55 (also known as decay accelerating factor) and the von Willebrand factor A (vWF-A) domain of factor B. Following a thorough assessment of the quality of the data, distances obtained from good-quality measurements are compared to predicted distances from a previously hypothesised model for the complex and are found to be incompatible. The success of using these distances as restraints in multi-body docking routines is presented critically.

KW - DEER

KW - distance restraints

KW - CD55

KW - vWF-A

KW - decay acceleration

KW - DECAY-ACCELERATING FACTOR

KW - PATHWAY C3 CONVERTASE

KW - DISTANCE MEASUREMENTS

KW - ALTERNATIVE PATHWAY

KW - ESCHERICHIA-COLI

KW - EPR SPECTROSCOPY

KW - NMR SYSTEM

KW - REFINEMENT

KW - MODEL

KW - BIOMACROMOLECULES

U2 - 10.1080/00268976.2013.827754

DO - 10.1080/00268976.2013.827754

M3 - Article

SN - 0026-8976

VL - 111

SP - 2865

EP - 2872

JO - Molecular Physics

JF - Molecular Physics

IS - 18-19

ER -

Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls

Abstract

Keywords

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Projects

Royal Society Research Fellowship: Royal Society Research Fellowship

Cite this