(Q28285338)

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The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues

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The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues (English)

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2

object named as

Reija Hieta

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5

object named as

Rik K Wierenga

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Johanna Myllyharju

6

object named as

Johanna Myllyharju

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author name string

Mira Pekkala

1

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Ulrich Bergmann

3

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Kari I Kivirikko

4

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language of work or name

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publication date

10 December 2004

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Journal of Biological Chemistry

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279

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50

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52255-61

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Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

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Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis

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A conserved family of prolyl-4-hydroxylases that modify HIF

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C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

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Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor

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Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme

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Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque.

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Prolyl 4-hydroxylase isoenzymes I and II have different expression patterns in several human tissues.

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Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase

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Collagens, modifying enzymes and their mutations in humans, flies and worms

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Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase

1 reference

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The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides

1 reference

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WW and SH3 domains, two different scaffolds to recognize proline-rich ligands

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Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly

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EVH1 domains: structure, function and interactions

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Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules

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Profilin binds proline-rich ligands in two distinct amide backbone orientations

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X-ray structure determination of human profilin II: A comparative structural analysis of human profilins

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Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase

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Design of Stable α-Helical Arrays from an Idealized TPR Motif

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TPR proteins: the versatile helix

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Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5

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Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

1 reference

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Mechanism of the Prolyl Hydroxylase Reaction. 2. Kinetic Analysis of the Reaction Sequence

1 reference

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The CCP4 suite: programs for protein crystallography

1 reference

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Automated MAD and MIR structure solution

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Improved methods for building protein models in electron density maps and the location of errors in these models

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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Refinement of macromolecular structures by the maximum-likelihood method

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PROCHECK: a program to check the stereochemical quality of protein structures

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ICM?A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation

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Dali/FSSP classification of three-dimensional protein folds

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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

1 reference

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Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)

1 reference

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Insights on the conformational stability of collagen

1 reference

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Host-guest scale of left-handed polyproline II helix formation.

1 reference

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Stereospecific interactions of proline residues in protein structures and complexes

1 reference

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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

1 reference

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

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21 January 2018

Identifiers

10.1074/JBC.M410007200

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