Structures of the rat complement regulator CrrY

Pietro Roversi; Steven Johnson; Joseph J.E. Caesar; Florence McLean; Kirstin J. Leath; Stefanos A Tsiftsoglou; B. Paul Morgan; Claire L. Harris; Robert B. Sim; Susan M. Lea

doi:10.1107/S1744309111016551

Structures of the rat complement regulator CrrY

Pietro Roversi, Steven Johnson, Joseph J.E. Caesar, Florence McLean, Kirstin J. Leath, Stefanos A Tsiftsoglou, B. Paul Morgan, Claire L. Harris, Robert B. Sim, Susan M. Lea

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

6 Citations (Scopus)

Abstract

Complement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70° bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b.

Original language	English
Pages (from-to)	739-743
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	67
Issue number	7
DOIs	https://doi.org/10.1107/S1744309111016551
Publication status	Published - Jul 2011
Externally published	Yes

Keywords

CCP
complement regulator
CrrY
rat

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10.1107/S1744309111016551

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title = "Structures of the rat complement regulator CrrY",

abstract = "Complement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70° bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b.",

keywords = "CCP, complement regulator, CrrY, rat",

author = "Pietro Roversi and Steven Johnson and Caesar, \{Joseph J.E.\} and Florence McLean and Leath, \{Kirstin J.\} and Tsiftsoglou, \{Stefanos A\} and Morgan, \{B. Paul\} and Harris, \{Claire L.\} and Sim, \{Robert B.\} and Lea, \{Susan M.\}",

year = "2011",

month = jul,

doi = "10.1107/S1744309111016551",

language = "English",

volume = "67",

pages = "739--743",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

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T1 - Structures of the rat complement regulator CrrY

AU - Roversi, Pietro

AU - Johnson, Steven

AU - Caesar, Joseph J.E.

AU - McLean, Florence

AU - Leath, Kirstin J.

AU - Tsiftsoglou, Stefanos A

AU - Morgan, B. Paul

AU - Harris, Claire L.

AU - Sim, Robert B.

AU - Lea, Susan M.

PY - 2011/7

Y1 - 2011/7

N2 - Complement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70° bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b.

AB - Complement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70° bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b.

KW - CCP

KW - complement regulator

KW - CrrY

KW - rat

UR - http://www.scopus.com/inward/record.url?scp=79960932878&partnerID=8YFLogxK

U2 - 10.1107/S1744309111016551

DO - 10.1107/S1744309111016551

M3 - Article

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AN - SCOPUS:79960932878

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SP - 739

EP - 743

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 7

ER -

Structures of the rat complement regulator CrrY

Abstract

Keywords

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