scholarly journals Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutions

1989 ◽  
Vol 261 (1) ◽  
pp. 253-257 ◽  
Author(s):  
A T Baker ◽  
J A M Ramshaw ◽  
D Chan ◽  
W G Cole ◽  
J F Bateman
Keyword(s):  
Osteogenesis Imperfecta ◽  
Molecular Modelling ◽  
Triple Helix ◽  
Structural Abnormality ◽  
Denaturation Temperature ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Helix Structure ◽  
Collagen Stability

The effect of glycine-to-arginine mutations in the alpha 1 (I)-chain on collagen triple-helix structure in lethal perinatal osteogenesis imperfecta was studied by determination of the helix denaturation temperature and by computerized molecular modelling. Arginine substitutions at glycine residues 391 and 667 resulted in similar small decreases in helix stability. Molecular modelling suggested that the glycine-to-arginine-391 mutant resulted in only a relatively small localized disruption to the helix structure. Thus the glycine-to-arginine substitutions may lead to only a small structural abnormality of the collagen helix, and it is most likely that the over-modification of lysine, poor secretion, increased degradation and other functional sequelae result from a kinetic defect in collagen helix formation resulting from the mutation.

Determination of G*G.cntdot.C triple-helix structure by molecular modeling and vibrational spectroscopy

1993 ◽  
Vol 115 (10) ◽  
pp. 4264-4270 ◽  
Author(s):  
Mohammed Ouali ◽  
Richard Letellier ◽  
Jian Sheng Sun ◽  
Alain Akhebat ◽  
Frederic Adnet ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Vibrational Spectroscopy ◽  
Triple Helix ◽  
Helix Structure

The collagen triple-helix structure

1997 ◽  
Vol 15 (8-9) ◽  
pp. 545-554 ◽  
Author(s):  
Barbara Brodsky ◽  
John A.M. Ramshaw
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Structure

Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix

1994 ◽  
Vol 3 (12) ◽  
pp. 2201-2206 ◽  
Author(s):  
A. Forlino ◽  
F. Zolezzi ◽  
M. Valli ◽  
P.F. Pignatti ◽  
G. Cetta ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Triple Helix ◽  
Central Domain ◽  
Type Iii ◽  
Collagen Triple Helix ◽  
Severe Type

Elucidating pH-Dependent Collagen Triple Helix Formation through Interstrand Hydroxyproline-Glutamic Acid Interactions

ChemBioChem ◽  
2014 ◽  
Vol 16 (3) ◽  
pp. 407-410 ◽  
Author(s):  
Liwei Chen ◽  
Shuting Cai ◽  
Jaehong Lim ◽  
Su Seong Lee ◽  
Song-Gil Lee
Keyword(s):  
Glutamic Acid ◽  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation ◽  
Ph Dependent

scholarly journals Structural Heterogeneity of Type I Collagen Triple Helix and Its Role in Osteogenesis Imperfecta

2007 ◽  
Vol 283 (8) ◽  
pp. 4787-4798 ◽  
Author(s):  
Elena Makareeva ◽  
Edward L. Mertz ◽  
Natalia V. Kuznetsova ◽  
Mary B. Sutter ◽  
Angela M. DeRidder ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Triple Helix ◽  
Type I Collagen ◽  
Structural Heterogeneity ◽  
Type I ◽  
Collagen Triple Helix

scholarly journals Collagen Triple Helix Formation Can Be Nucleated at Either End

2003 ◽  
Vol 278 (10) ◽  
pp. 7747-7750 ◽  
Author(s):  
Sabine Frank ◽  
Sergei Boudko ◽  
Kazunori Mizuno ◽  
Therese Schulthess ◽  
Jürgen Engel ◽  
...  
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation

scholarly journals Characterization of three osteogenesis imperfecta collagen α 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity

1992 ◽  
Vol 288 (1) ◽  
pp. 131-135 ◽  
Author(s):  
J F Bateman ◽  
I Moeller ◽  
M Hannagan ◽  
D Chan ◽  
W G Cole
Keyword(s):  
Osteogenesis Imperfecta ◽  
Triple Helix ◽  
Type I Collagen ◽  
Type I ◽  
Disruptive Effect ◽  
Collagen Triple Helix ◽  
C Terminus ◽  
Glycine Substitution ◽  
C And N

Type I collagen alpha 1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI). The Gly substitutions displayed a gradient of phenotypic severity according to the location of the mutation in the collagen triple helix. The most C-terminal of these, Gly565 to Ser, led to the lethal perinatal (type II) form of OI, whereas the more N-terminal mutations, Gly415 and Gly352 to Ser, led to severe OI (type III/IV) and moderate OI (type IVB) respectively. These data support the notion that glycine substitutions towards the C-terminus of the alpha 1(I) or alpha 2(I) chains will be more clinically severe than those towards the N-terminus. This results from the more disruptive effect of the mutations at the C-terminus on helix initiation and C- and N-terminal helix directional propagation. This generalization must be modified by considering the nature of the glycine substitution and the surrounding amino acid sequence, since the helix is composed of subdomains of differing stability which will affect the ability of helix re-nucleation and propagation.

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