3hr2 | pdb_00003hr2

Low resolution, molecular envelope structure of type I collagen in situ determined by fiber diffraction. Single type I collagen molecule, post rigid body refinement, 'relaxed'

spinqualitylabelsall models 3hr2, resolution 5.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hr2 is a 3 chain structure with sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1y0f. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: HYP, LYZ Related: 1y0f, 3hqv Resources: FirstGlance, OCA, RCSB, PDBsum Function [CO1A1_RAT] Type I collagen is a member of group I collagen (fibrillar forming collagen). [CO1A2_RAT] Type I collagen is a member of group I collagen (fibrillar forming collagen). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a approximately 40.0 A, b approximately 27.0 A, c approximately 678 A, alpha approximately 89.2 degrees , beta approximately 94.6 degrees , gamma approximately 105.6 degrees ; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 A axial and 11.1 A equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase. Microfibrillar structure of type I collagen in situ.,Orgel JP, Irving TC, Miller A, Wess TJ Proc Natl Acad Sci U S A. 2006 Jun 13;103(24):9001-5. Epub 2006 Jun 2. PMID:16751282 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Collagen

Proteopedia Page Contributors and Editors (what is this?)

OCA