Localization of flexible sites in thread-like molecules from electron micrographs

Hofmann, H; Voss, Tilman; Kühn, Klaus; Engel, Jürgen

doi:10.1016/s0022-2836(84)80029-7

Cited by 256 publications

(128 citation statements)

References 32 publications

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“…The frequency of these interruptions is higher in the N-terminal portion which also contains the large non-helical areas. These findings correlate well with earlier electron microscopical observations which revealed the highest flexibility of the type IV collagen molecule in the N-terminal third of the triple-helical domain [37].…”

Section: R G P P C C Q C P~c L~g P P C I K~e K G F P G~p G~dsupporting

confidence: 92%

“…Pepsin treatment cleaves the a2(IV) chain in the loop region between Gln-678 and Glu-679 (in Fig. 3) thus leading to the early pepsin fragment ol2(IV) 70 kDa which, however, appears only after reduction of the disulfide bridge [37]. In contrast, the al(1V) chain remains intact in this region.…”

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

“…To obtain maximal length of the adjacent triple-helical sections we have introduced a gap of seven residues into the al(1V) chain. In the electron microscope this area can be seen as an extraordinarily flexible region about 30 nm away from the 7s overlap region [37]. Cleavage by pepsin in interruption I11 leads to the fragments al(1V) 140 kDa and a2(IV) 120 kDa Interruption X (seven residues long) is the next main peptic cleavage site which is located 70 nm further to the C terminus.…”

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

“…This may in part be due to the stabilizing effect of the tetrameric 7s complex, in spite of the fact that the intermolecular crosslinks which connect the 30-nm overlapping molecules are more than 30 residues away (Fig.3). On the other hand, there is electron microscopical evidence for a secondary structure of this area which forces the molecules to a kink of 40" [37].…”

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

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Human basement membrane collagen (type IV)

Brazel

Pollner

Oberbäumer

et al. 1988

European Journal of Biochemistry

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The cDNA and protein sequences of the N-terminal6OY0 of the a2(IV) chain of human basement membrane collagen have been determined. By repeated primer extension with synthetic oiigodeoxynucleotides and mRNA from either HT1080 cells or human placenta overlapping clones were obtained which cover 3414 bp. The derived protein sequence allows for the first time a comparison and alignment of both a chains of type IV collagen from the N terminus. This alignment reveals an additional 43 amino acid residues in the a2(IV) chain as compared to the al(1V) chain. 21 of these additional residues form a disulfide-bridged loop within the triple helix which is unique among all known collagens.

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Section: R G P P C C Q C P~c L~g P P C I K~e K G F P G~p G~dsupporting

confidence: 92%

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

Section: K P G P R G K P G I D G D K G E K G S I G P P G E P G Y P D mentioning

confidence: 99%

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Human basement membrane collagen (type IV)

Brazel

Pollner

Oberbäumer

et al. 1988

European Journal of Biochemistry

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“…Some interruptions are known to play a role in binding to tumor cell integrins 12 or as specific sites of matrix metalloproteinase cleavage, 33 and they have been suggested to represent flexible or kink sites involved in the network structure of Type IV collagen. [34][35][36] A total of 354 interruptions are found in all human nonfibrillar collagens and these can been classified according to number of residues within the interruption which are flanked by (Gly-X-Y) n triplets 37,38 (Figure 3). The repeating (Gly-X-Y) n sequence generates a pattern with two amino acids between Gly residues.…”

Section: Natural Interruptions In the Gly-x-y Repeating Pattern In Nomentioning

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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Protein Composites: Biominerals

Veis

2003

Biopolymers Online

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Introduction Historical Outline Type I Collagen Synthesis and Secretion Molecular Structure and Fibril Assembly Chemistry of Collagen Crosslinking Matrix Mineralization and Organization Tooth Enamel Invertebrate Mineralization and Organization Outlook and Perspectives Acknowledgments

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Localization of flexible sites in thread-like molecules from electron micrographs

Cited by 256 publications

References 32 publications

Human basement membrane collagen (type IV)

Human basement membrane collagen (type IV)

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

Protein Composites: Biominerals

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