(1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7

Marie M. Phelan; Chuong-Thu Thai; Andrew P. Herbert; Juraj Bella; Dusan Uhrin; Ronald T. Ogata; Paul N. Barlow; Janice Bramham

doi:10.1007/s12104-008-9139-z

(1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7

Marie M. Phelan, Chuong-Thu Thai, Andrew P. Herbert, Juraj Bella, Dusan Uhrin, Ronald T. Ogata, Paul N. Barlow, Janice Bramham

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

Abstract

The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the 1H, 15N and 13C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.

Original language	English
Pages (from-to)	49-52
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	3
Issue number	1
DOIs	https://doi.org/10.1007/s12104-008-9139-z
Publication status	Published - Jun 2009

Keywords

Complement
Membrane attack complex
MAC
C7
Factor I module
FIM
NMR
Resonance assignment

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10.1007/s12104-008-9139-z

http://www.springerlink.com/content/l702555n756720w2/

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title = "(1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7",

abstract = "The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the 1H, 15N and 13C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.",

keywords = "Complement , Membrane attack complex, MAC , C7, Factor I module , FIM, NMR, Resonance assignment",

author = "Phelan, {Marie M.} and Chuong-Thu Thai and Herbert, {Andrew P.} and Juraj Bella and Dusan Uhrin and Ogata, {Ronald T.} and Barlow, {Paul N.} and Janice Bramham",

year = "2009",

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doi = "10.1007/s12104-008-9139-z",

language = "English",

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T1 - (1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7

AU - Phelan, Marie M.

AU - Thai, Chuong-Thu

AU - Herbert, Andrew P.

AU - Bella, Juraj

AU - Uhrin, Dusan

AU - Ogata, Ronald T.

AU - Barlow, Paul N.

AU - Bramham, Janice

PY - 2009/6

Y1 - 2009/6

N2 - The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the 1H, 15N and 13C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.

AB - The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the 1H, 15N and 13C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.

KW - Complement

KW - Membrane attack complex

KW - MAC

KW - C7

KW - Factor I module

KW - FIM

KW - NMR

KW - Resonance assignment

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U2 - 10.1007/s12104-008-9139-z

DO - 10.1007/s12104-008-9139-z

M3 - Article

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VL - 3

SP - 49

EP - 52

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

SN - 1874-2718

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ER -

(1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7

Abstract

Keywords

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