Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL OF HUMAN NIDOGEN YWTD BETA-PROPELLER DOMAINTHEORETICAL MODEL OF HUMAN NIDOGEN YWTD BETA-PROPELLER DOMAIN

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

An abundant, widely dispersed, extracellular sequence repeat that contains a consensus YWTD motif is shown here to occur in groups of six contiguous repeats. Thirteen lines of evidence, including experimental and computational data, predict with p<3x10(-9) that the repeats do not form tandem domains, but rather each group of six repeats folds into a compact beta-propeller structure. The six beta-sheets are arranged about a 6-fold pseudosymmetry axis, and each repeat contributes loops to the faces surrounding the pseudosymmetry axis. Seven different endocytic receptors that contain from one to eight YWTD beta-propeller domains act as lipoprotein, vitellogenin, and scavenger receptors. In the low density lipoprotein receptor (LDLR), the many mutations in familial hypercholesterolaemia that map to the YWTD domain can now be interpreted. In the extracellular matrix component nidogen, the YWTD domain functions to bind laminin. Three YWTD domains and interspersed fibronectin type III (FN3) domains constitute almost the entire extracellular domain of the sevenless and c-ros receptor tyrosine kinases. YWTD domains often are bounded by epidermal growth factor (EGF) modules, including in the EGF precursor itself. YWTD beta-propellers have a circular folding pattern that brings neighboring modules into close proximity, and may have important consequences for the architecture of multi-domain proteins.

An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.,Springer TA J Mol Biol. 1998 Nov 6;283(4):837-62. PMID:9790844[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Springer TA. An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components. J Mol Biol. 1998 Nov 6;283(4):837-62. PMID:9790844 doi:10.1006/jmbi.1998.2115
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA