Imino Acids and Collagen Triple Helix Stability:  Characterization of Collagen-like Polypeptides Containing Hyp-Hyp-Gly Sequence Repeats

2004 ◽  
Vol 126 (37) ◽  
pp. 11402-11403 ◽  
Author(s):  
Rita Berisio ◽  
Vincenzo Granata ◽  
Luigi Vitagliano ◽  
Adriana Zagari
Biochemistry ◽  
2005 ◽  
Vol 44 (5) ◽  
pp. 1414-1422 ◽  
Author(s):  
Anton V. Persikov ◽  
John A. M. Ramshaw ◽  
Alan Kirkpatrick ◽  
Barbara Brodsky

2011 ◽  
Vol 508 (1) ◽  
pp. 46-53 ◽  
Author(s):  
Chia-Ching Chen ◽  
Wei Hsu ◽  
Kuo-Chu Hwang ◽  
Jih Ru Hwu ◽  
Chun-Cheng Lin ◽  
...  

Biochemistry ◽  
2002 ◽  
Vol 41 (25) ◽  
pp. 8143-8151 ◽  
Author(s):  
Yujia Xu ◽  
Manjiri Bhate ◽  
Barbara Brodsky

2019 ◽  
Vol 123 (34) ◽  
pp. 7354-7364 ◽  
Author(s):  
Michele Cutini ◽  
Massimo Bocus ◽  
Piero Ugliengo

1992 ◽  
Vol 288 (1) ◽  
pp. 131-135 ◽  
Author(s):  
J F Bateman ◽  
I Moeller ◽  
M Hannagan ◽  
D Chan ◽  
W G Cole

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.


2007 ◽  
Vol 13 (10) ◽  
pp. 2966-2973 ◽  
Author(s):  
Ulrike Kusebauch ◽  
Sergio A. Cadamuro ◽  
Hans-Jürgen Musiol ◽  
Luis Moroder ◽  
Christian Renner

2017 ◽  
Vol 18 (4) ◽  
pp. 1157-1161 ◽  
Author(s):  
Amanda M. Acevedo-Jake ◽  
Daniel H. Ngo ◽  
Jeffrey D. Hartgerink

2012 ◽  
Vol 13 (5) ◽  
pp. 1250-1258 ◽  
Author(s):  
Catarina I. F. Silva ◽  
Paulina J. Skrzeszewska ◽  
Monika D. Golinska ◽  
Marc W. T. Werten ◽  
Gerrit Eggink ◽  
...  

1991 ◽  
Vol 115 (4) ◽  
pp. 1159-1169 ◽  
Author(s):  
E M Kurz ◽  
T W Holstein ◽  
B M Petri ◽  
J Engel ◽  
C N David

We have isolated and characterized four collagen-related c-DNA clones (N-COL 1, N-COL 2, N-COL 3, N-COL 4) that are highly expressed in developing nematocytes in hydra. All four c-DNAs as well as their corresponding transcripts are small in size (600-1,000 bp). The deduced amino acid sequences show that they contain a central region consisting of 14 to 16 Gly-X-Y triplets. This region is flanked amino-terminal by a stretch of 14-23 proline residues and carboxy-terminal by a stretch of 6-9 prolines. At the NH2- and COOH-termini are repeated patterns of cysteine residues that are highly conserved between the molecules. A model is proposed which consists of a central stable collagen triple helix of 12-14 nm length from which three 9-22 nm long polyproline II type helices emerge at both ends. Disulfide linkage between cysteine-rich segments in these helices could lead to the formation of oligomeric network structures. Electrophoretic characterization of nematocyst extracts allows resolution of small proline-rich polypeptides that correspond in size to the cloned sequences.


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