Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10

Okuyama, Kenji; Okuyama, Keiji; Arnott, Struther; Takayanagi, Motowo; Kakudo, Masao

doi:10.1016/0022-2836(81)90252-7

Cited by 171 publications

(145 citation statements)

References 19 publications

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“…The first crystal structure was obtained by Okuyama et al (1981) 17 for (Pro-Pro-Gly) 10 , followed by structures for peptides with varying sequences from a number of laboratories (Table I) (for reviews, see 15 ). In addition to the peptide structures, there are high resolution structures of complexes of a triple-helical peptide bound to the I domain of integrin 19 and one bound to a bacterial cell surface receptor.…”

Section: X-ray Crystallography Of Triple-helical Peptidesmentioning

confidence: 99%

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

et al. 2008

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Peptides have been an integral part of the collagen triple‐helix structure story, and have continued to serve as useful models for biophysical studies and for establishing biologically important sequence‐structure‐function relationships. High resolution structures of triple‐helical peptides have confirmed the basic Ramachandran triple‐helix model and provided new insights into the hydration, hydrogen bonding, and sequence dependent helical parameters in collagen. The dependence of collagen triple‐helix stability on the residues in its (Gly‐X‐Y)n repeating sequence has been investigated by measuring melting temperatures of host‐guest peptides and an on‐line collagen stability calculator is now available. Although the presence of Gly as every third residue is essential for an undistorted structure, interruptions in the repeating (Gly‐X‐Y)n amino acid sequence pattern are found in the triple‐helical domains of all nonfibrillar collagens, and are likely to play a role in collagen binding and degradation. Peptide models indicate that small interruptions can be incorporated into a rod‐like triple‐helix with a highly localized effect, which perturbs hydrogen bonds and places the standard triple‐helices on both ends out of register. In contrast to natural interruptions, missense mutations which replace one Gly in a triple‐helix domain by a larger residue have pathological consequences, and studies on peptides containing such Gly substitutions clarify their effect on conformation, stability, and folding. Recent studies suggest peptides may also be useful in defining the basic principles of collagen self‐association to the supramolecular structures found in tissues. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 345–353, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Section: X-ray Crystallography Of Triple-helical Peptidesmentioning

confidence: 99%

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

et al. 2008

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“…10,12 The amide I peak of this collagen helix is characteristically above 1658-1660 cm − 1 , appearing in deconvoluted or second-derivative spectra as three distinct bands at 1657-1661, 1630-37 cm − 1 , and above 1670 cm − 1 . 23,31,32,[35][36][37] These bands appear to be characteristic of a triple helix and also occur in other molecules that contain a collagen-like triple helix, including the nonfibrillar collagens that contain one or several small triplehelical domains interrupted by short nonhelical domains, and the complement component C1q that comprises a collagen-like triple helix at the N-terminus, with C-terminal globular heads. 38 In all these proteins, the band at 1657-61 cm − 1 is normally the strongest of the three.…”

Section: Discussionmentioning

confidence: 99%

Chemical changes demonstrated in cartilage by synchrotron infrared microspectroscopy in an antibody-induced murine model of rheumatoid arthritis

et al. 2011

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Abstract. Collagen antibody-induced arthritis develops in mice following passive transfer of monoclonal antibodies (mAbs) to type II collagen (CII) and is attributed to effects of proinflammatory immune complexes, but transferred mAbs may react directly and damagingly with CII. To determine whether such mAbs cause cartilage damage in vivo in the absence of inflammation, mice lacking complement factor 5 that do not develop joint inflammation were injected intravenously with two arthritogenic mAbs to CII, M2139 and CIIC1. Paws were collected at day 3, decalcified, paraffin embedded, and 5-μm sections were examined using standard histology and synchrotron Fourier-transform infrared microspectroscopy (FTIRM). None of the mice injected with mAb showed visual or histological evidence of inflammation but there were histological changes in the articular cartilage including loss of proteoglycan and altered chondrocyte morphology. Findings using FTIRM at high lateral resolution revealed loss of collagen and the appearance of a new peak at 1635 cm − 1 at the surface of the cartilage interpreted as cellular activation. Thus, we demonstrate the utility of synchrotron FTIRM for examining chemical changes in diseased cartilage at the microscopic level and establish that arthritogenic mAbs to CII do cause cartilage damage in vivo in the absence of inflammation. C 2011 Society of Photo-Optical Instrumentation Engineers (SPIE).

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“…[36][37][38][39] The assembly of collagen molecules into fibrils is an entropy driven process, similar to that occurring in other protein self-assembly systems, such as microtubules. 20,23,24,40,41 These processes are driven by the loss of solvent molecules from the surface of protein molecules and result in assemblies with a circular cross section, which minimizes the surface area/volume ratio of the final assembly. Although the broad principles of collagen fibril self-assembly are generally accepted, less is known about the molecular mechanisms of the assembly process.…”

Section: Collagenmentioning

confidence: 99%

Genetically Modified Collagen‐like Triple Helix Peptide as Biomimetic Template THIS CHAPTER HAS BEEN RETRACTED

Kaur

Bai

Matsui

2011

Hybrid Nanomaterials

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Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10

Cited by 171 publications

References 19 publications

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

Chemical changes demonstrated in cartilage by synchrotron infrared microspectroscopy in an antibody-induced murine model of rheumatoid arthritis

Genetically Modified Collagen‐like Triple Helix Peptide as Biomimetic Template THIS CHAPTER HAS BEEN RETRACTED

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