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Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
title
Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r
(English)
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
main subject
Complement C1r
1 reference
stated in
GOA release 2020-03-11
zymogen activation
1 reference
stated in
GOA release 2020-03-11
author
Péter Závodszky
series ordinal
5
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József Kardos
object named as
József Kardos
series ordinal
2
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Katalin Adrienna Kékesi
object named as
Katalin Adrienna Kékesi
series ordinal
3
0 references
author name string
Balázs Major
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
Zsolt Lorincz
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
Péter Gál
series ordinal
6
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
language of work or name
English
0 references
publication date
16 April 2010
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
published in
Journal of Biological Chemistry
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
volume
285
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stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
page(s)
11863–11869
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stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
issue
16
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
cites work
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MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity
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Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r
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Cytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramer
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The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
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X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement
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Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism
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16 March 2017
The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
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PubMed Central
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Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle
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16 March 2017
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family
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The evolving model of calmodulin structure, function and activation
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Ca2+ binding properties and Ca2(+)-dependent interactions of the isolated NH2-terminal alpha fragments of human complement proteases C1-r and C1-s
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Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions
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Identification of the C1q-binding Sites of Human C1r and C1s: a refined three-dimensional model of the C1 complex of complement
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Assembly of C1 and the MBL- and ficolin-MASP complexes: structural insights.
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The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
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The N-terminal CUB-epidermal growth factor module pair of human complement protease C1r binds Ca2+ with high affinity and mediates Ca2+-dependent interaction with C1s.
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Activation of human complement serine-proteinase C1r is down-regulated by a Ca(2+)-dependent intramolecular control that is released in the C1 complex through a signal transmitted by C1q.
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RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion.
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21 January 2018
The role of the individual domains in the structure and function of the catalytic region of a modular serine protease, C1r.
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21 January 2018
Assembly and enzymatic properties of the catalytic domain of human complement protease C1r.
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Crossref
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The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
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Crossref
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21 January 2018
Domain stability and metal-induced folding of calcium- and integrin-binding protein 1
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20178990
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Sequence Data Analysis for Long Disordered Regions Prediction in the Calcineurin Family
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20178990
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Molecular characterization of the catalytic domains of human complement serine protease C1r
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20178990
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Human complement serine proteases C1r and C1s and their proenzymes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20178990
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Predicting Protein Disorder for N-, C-, and Internal Regions
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20178990
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1074/JBC.M109.098541
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
PMCID
2852923
0 references
PubMed ID
20178990
1 reference
stated in
PubMed
PubMed ID
20178990
retrieved
7 March 2017
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