Type VII Collagen Specifically Binds Fibronectin via a Unique Subdomain Within the Collagenous Triple Helix
نویسندگان
چکیده
منابع مشابه
Understanding and Engineering the Collagen Triple Helix
UNDERSTANDING AND ENGINEERING THE COLLAGEN TRIPLE HELIX Matthew Donald Shoulders Under the supervision of Professor Ronald T. Raines At the University of Wisconsin-Madison This thesis presents a hypothesis-driven approach to collagen research that integrates the power of organic chemistry with the tools of biophysics to enhance our understanding of proline conformation and collagen structure an...
متن کاملThioamides in the collagen triple helix.
To probe noncovalent interactions within the collagen triple helix, backbone amides were replaced with a thioamide isostere. This subtle substitution is the first in the collagen backbone that does not compromise thermostability. A triple helix with a thioamide as a hydrogen bond donor was found to be more stable than triple helices assembled from isomeric thiopeptides.
متن کاملMacrocyclic scaffold for the collagen triple helix.
[structure: see text] Three strands of natural collagen are linked by covalent bonds prior to their folding into a triple helix. We report on a synthetic collagen in which the strands are pendent on a rigid macrocyclic scaffold of C(3) symmetry. The scaffold confers substantial conformational stability upon the collagen triple helix and makes its folding independent of concentration, both desir...
متن کاملCTHRC1 (Collagen Triple Helix Repeat Containing 1)
Collagen Triple Helix Repeat Containing-1, CTHRC1, is a 30kDa secreted protein that has the ability to inhibit collagen matrix synthesis. CTHRC1 is glycosylated and retains a signal sequence consistent with it being secreted from the cell. Activity of the protein is reliant on removal of the propeptide and while CTHRC1 does not contain a predictable consensus propeptide cleavage site, there is ...
متن کاملA statistically derived parameterization for the collagen triple-helix.
The triple-helix is a unique secondary structural motif found primarily within the collagens. In collagen, it is a homo- or hetero-tripeptide with a repeating primary sequence of (Gly-X-Y)(n), displaying characteristic peptide backbone dihedral angles. Studies of bulk collagen fibrils indicate that the triple-helix must be a highly repetitive secondary structure, with very specific constraints....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Investigative Dermatology
سال: 1994
ISSN: 0022-202X
DOI: 10.1111/1523-1747.ep12398270