Stabilization of short collagen-like triple helices by protein engineering

Frank, Stefanie; Kammerer, Richard A.; Mechling, Diane E.; Schulthess, Therese; Landwehr, Ruth; Bann, James G.; Guo, Yuan; Lustig, Ariel; Bächinger, Hans Peter; Engel, Jürgen

doi:10.1006/jmbi.2001.4644

Cited by 181 publications

(196 citation statements)

References 17 publications

Supporting

Mentioning

187

Contrasting

Order By: Relevance

“…In particular, members of the serpin family are highly conformationally mobile. It is also true that "model" peptides such as (PPG) 10 that are used throughout the study of collagen-binding proteins are not conformationally static (1,2,47). Indeed the oligomerization state of (PPG) 10 varies with both concentration and temperature.…”

Section: Discussionmentioning

confidence: 99%

The Molecular Interactions of Heat Shock Protein 47 (Hsp47) and Their Implications for Collagen Biosynthesis

Dafforn

Della

Miller

2001

Journal of Biological Chemistry

108

View full text Add to dashboard Cite

Heat shock protein 47 (Hsp47) is a procollagen/collagen-specific molecular chaperone protein derived from the serpin family of proteins and essential for the early stages of collagen biosynthesis. In this paper, the results of an extensive biophysical analysis of mature recombinant mouse Hsp47 show the existence of both a structurally mesostable monomer with a 5-strand A-sheet and/or a hyperstable trimer; both states have biological activity. It is also demonstrated that Hsp47 is able to bind to a monomeric and partially folded conformation collagen mimic peptide (PPG) 10

show abstract

Section: Discussionmentioning

confidence: 99%

The Molecular Interactions of Heat Shock Protein 47 (Hsp47) and Their Implications for Collagen Biosynthesis

Dafforn

Della

Miller

2001

Journal of Biological Chemistry

108

View full text Add to dashboard Cite

show abstract

“…The wavelength spectra represent at least an average of 10 scans with 0.1-nm resolution. The CD data were analyzed with SCIENTIST for Windows (MicroMath Research, St. Louis, MO) using the cubic equation for the all-or-none model described in Frank et al (42).…”

Section: Methodsmentioning

confidence: 99%

“…The heating rate was 7.5°C/h, and the data were collected using the software provided by the manufacturer. The data were analyzed using the cubic equation for the all-or-none model described in Frank et al (42).…”

Section: Methodsmentioning

confidence: 99%

Hydroxylation-induced Stabilization of the Collagen Triple Helix

Mizuno

Hayashi

Peyton

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

The collagen triple helix is one of the most abundant protein motifs in animals. The structural motif of collagen is the triple helix formed by the repeated sequence of -Gly-Xaa-Yaa-. Previous reports showed that H-(Pro-4(R)Hyp-Gly) 10 -OH (where '4(R)Hyp' is (2S,4R)-4-hydroxyproline) forms a trimeric structure, whereas H-(4(R)Hyp-Pro-Gly) 10 -OH does not form a triple helix. Compared with H-(Pro-Pro-Gly) 10 -OH, the melting temperature of H-(Pro-4(R)Hyp-Gly) 10 -OH is higher, suggesting that 4(R)Hyp in the Yaa position has a stabilizing effect. The inability of triple helix formation of H-(4(R)Hyp-Pro-Gly) 10 -OH has been explained by a stereoelectronic effect, but the details are unknown. In this study, we synthesized a peptide that contains 4(R)Hyp in both the Xaa and the Yaa positions, that is, Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 and compared it to Ac-(GlyPro-4(R)Hyp) 10 -NH 2 , and Ac-(Gly-4(R)Hyp-Pro) 10 -NH 2 . Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 showed a polyproline II-like circular dichroic spectrum in water. The thermal transition temperatures measured by circular dichroism and differential scanning calorimetry were slightly higher than the values measured for Ac-(Gly-Pro-4(R)Hyp) 10 -NH 2 under the same conditions. For Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 , the calorimetric and the van't Hoff transition enthalpy ⌬H were significantly smaller than that of Ac-(Gly-Pro-4(R)Hyp) 10 -NH 2 . We postulate that the denatured states of the two peptides are significantly different, with Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 forming a more polyproline II-like structure instead of a random coil. Two-dimensional nuclear Overhauser effect spectroscopy suggests that the triple helical structure of Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 is more flexible than that of Ac-(Gly-Pro-4(R)Hyp) 10 -NH 2 . This is confirmed by the kinetics of amide 1 H exchange with solvent deuterium of Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 , which is faster than that of Ac-(Gly-Pro-4(R)Hyp) 10 -NH 2 . The higher transition temperature of Ac-(Gly-4(R)Hyp-4(R)Hyp) 10 -NH 2 , can be explained by the higher trans/cis ratio of the Gly-4(R)Hyp peptide bonds than that of the Gly-Pro bonds, and this ratio compensates for the weaker interchain hydrogen bonds.The collagen triple helix is one of the most abundant protein motifs in animals. Each of the three polypeptide chains forms a polyproline-II like structure, and these structures twist around each other to form a right-handed superhelix (1, 2). To form this structure, a sequence with Gly in every third position is required. The general sequence is -Gly-Xaa-Yaa-, and the Xaa and Yaa positions contain a high content of proline and hydroxyproline. Twenty-seven types of collagens and more than fifteen proteins that form a triple helix, but are not named collagens such as collectins, ficolins, and scavenger receptors (3-5), occur in humans. In vertebrates, most of the proline residues in the Yaa position of the -Gly-Xaa-Yaa-repeated sequence are post-translationally modified to 4(R)Hyp 1 by prolyl 4-hydroxylase (EC 1.14.1...

show abstract

“…2B). To determine the role of the coiled coil in activation, we replaced the coiled-coil domain with a 27-amino acid trimerization domain, called foldon, from bacteriophage T4 fibritin (44). This construct, Crn1-foldon, activated Arp2/3 complex and recruited it to actin filaments similarly to wildtype coronin (Figs.…”

Section: Low Concentrations Of Crn1 Recruit Arp2/3 Complex To Actin Fmentioning

confidence: 99%

Mechanism of a Concentration-dependent Switch between Activation and Inhibition of Arp2/3 Complex by Coronin

Liu¹,

Needham²,

May

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Stabilization of short collagen-like triple helices by protein engineering

Cited by 181 publications

References 17 publications

The Molecular Interactions of Heat Shock Protein 47 (Hsp47) and Their Implications for Collagen Biosynthesis

The Molecular Interactions of Heat Shock Protein 47 (Hsp47) and Their Implications for Collagen Biosynthesis

Hydroxylation-induced Stabilization of the Collagen Triple Helix

Mechanism of a Concentration-dependent Switch between Activation and Inhibition of Arp2/3 Complex by Coronin

Contact Info

Product

Resources

About