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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003965naa a2200433 4500
001oai:lup.lub.lu.se:47590ebc-912d-49c6-a04f-0f2033d86b7a
003SwePub
008160401s2004 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/2752492 URI
024a https://doi.org/10.1016/j.jmb.2004.03.0422 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Kassner, A4 aut
2451 0a Molecular structure and interaction of recombinant human type XVI collagen
264 1b Elsevier BV,c 2004
520 a Collagen XVI is a minor component of at least two different extracellular fibrillar networks of specialized regions of skin and cartilage. In skin, collagen XVI is integrated into particular fibrillin-rich microfibrils lacking an amorphous elastin core. In cartilage, collagen XVI is a component of small heterotypic D-banded fibrils, mainly occurring in the territorial matrix of chondrocytes. Here, we present the first direct evidence for the molecular structure and functional properties of these fibril-associated collagens with interrupted triple helices (FACIT). We have expressed recombinantly the full-length alpha1 chain of human collagen XVI in HEK 293 EBNA cells in large quantities using an episomal expression system. Secreted full-length recombinant collagen XVI forms stable disulfide-bonded homotrimers and is rapidly proteolytically processed to distinct fragments at specific protease sequence motifs, one resembling an aggrecanase recognition site. Limited trypsin digestion assays and thermal transition curves imply sequential thermal denaturation of individual triple helical domains of this recombinant collagen, similar to authentic collagen XVI. Molecular images of collagen XVI reveal rod-like molecules which harbor multiple sharp kinks attributing a highly flexible structure presumably introduced by non-collagenous (NC) regions. Terminally located cloverleaf-shaped nodules correspond to the large NC NC11 domain of trimeric collagen XVI. The total length of individual trimeric recombinant collagen XVI molecules constitutes about 240 nm as calculated by atomic force and negative staining electron microscopy. Recombinant collagen XVI interacts with fibrillin-1 and with fibronectin indicating multiple molecular interactions in which this ubiquitously expressed and versatile FACIT-collagen can participate. In vitro generated collagen XVI provides an indispensable tool for future determination of its function during supramolecular assembly of matrix aggregates and its role in maintenance, organization and interaction of fibrillar structures. (C) 2004 Elsevier Ltd. All rights reserved.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Infektionsmedicin0 (SwePub)302092 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Infectious Medicine0 (SwePub)302092 hsv//eng
653 a collagen XVI
653 a FACIT
653 a molecular structure
653 a fibronectin
653 a recombinant
700a Tiedemann, K4 aut
700a Notbohm, M4 aut
700a Ludwig, T4 aut
700a Mörgelin, Matthiasu Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine4 aut0 (Swepub:lu)medk-mmn
700a Reinhardt, DP4 aut
700a Chu, ML4 aut
700a Bruckner, P4 aut
700a Grassel, S4 aut
710a Infektionsmedicinb Sektion III4 org
773t Journal of Molecular Biologyd : Elsevier BVg 339:4, s. 835-853q 339:4<835-853x 1089-8638x 0022-2836
856u http://dx.doi.org/10.1016/j.jmb.2004.03.042y FULLTEXT
8564 8u https://lup.lub.lu.se/record/275249
8564 8u https://doi.org/10.1016/j.jmb.2004.03.042

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