In molecular biology, the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, including type I collagen. In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently WebCOL4A1 (collagen type IV α 1 chain) belongs to the collagen family. It has an N-terminal 7S domain, a C-terminal globular domain (NC1), and the central triple helical part with short interruptions of the Gly-X-Y repeats [ 1]. It is an important constituent of type IV collagen in the basement membrane [ 2].
Collagen-like proteins of pathogenic streptococci - PubMed
WebGly-X-Y repeat) regions of collagen genes were generated by cloning PCR fragments encoding these regions into L4440 vector and transforming bacterial strain HT115 [17]. RAD-SMAD reporter and dbl-1 transcriptional reporter imaging . Fluorescence images were taken at 40x using a Zeiss Apotome microscope. For fluorescence WebThe Gly-X-Y repeat domains in certain proteins, including host defense proteins, make them adaptable to a range of protein assemblies (Ramshaw et al., 1998). It was speculated that amino acid ... show screen keyboard shortcut
Submissions for variant NM_000091.5(COL4A3):c.1372G>C …
WebMar 15, 2004 · They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC) ... Macromolecules Find similar proteins by: (by identity cutoff) 3D Structure WebThe molecular conformation of the collagen triple helix confers strict amino acid sequence constraints, requiring a (Gly-X-Y) (n) repeating pattern and a high content of imino acids. The increasing family of collagens and proteins with collagenous domains shows the collagen triple helix to be a basic motif adaptable to a range of proteins and ... WebThe variant disrupts a glycine residue in the canonical Gly-X-Y repeats of the triple helix domain, which are required for stability and structure of this protein. Therefore it is expected to severely affect the function of the protein. The frequency of this variant in the general population is consistent with pathogenicity. show screen