Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon (Q27640648)

2

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Margrit Jenny

3

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Therese Schulthess

4

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Richard A Kammerer

5

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Sergei Boudko

6

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Ruth Landwehr

7

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Kenji Okuyama

8

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Jürgen Engel

Collectin structure: a review

9

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publication date

March 2003

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published in

Structure

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volume

11

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issue

3

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page(s)

339-46

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cites work

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The triple helix in equilibrium with coil conversion of collagen-like polytripeptides in aqueous and nonaqueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n

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X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)

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Code for collagen's stability deciphered

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Insights on the conformational stability of collagen

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The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

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Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer

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Trimeric assembly and three-dimensional structure model of the FACIT collagen COL1-NC1 junction from CD and NMR analysis

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A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins

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Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization

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Folding of collagen IV

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A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation

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Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from third to first order kinetics

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The fibrillar collagens, collagen VIII, collagen X and the C1q complement proteins share a similar domain in their C-terminal non-collagenous regions

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Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution

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