File:Heparin binding sites on TGF-β superfamily cytokines.png

From Wikimedia Commons, the free media repository
Jump to navigation Jump to search

Original file (1,437 × 923 pixels, file size: 695 KB, MIME type: image/png)

Captions

Captions

Add a one-line explanation of what this file represents

Summary

[edit]
Description

Figure 2. Heparin binding sites on TGF-β superfamily cytokines. Protein chains are shown as in Figure 1, and heparin binding site basic residues are shown in brown stick format. (A) The dimer of TGF-β1 (co-ordinates from 1KLC.pdb). Residues K25, R26, K31, K37, R94 and R97 form a discontinuous heparin binding site at the tips of the “fingers” [13]. (B) Sclerostin monomer (one of the NMR ensemble in 2K8P.pdb) with heparin-binding residues in brown. Cystine residues are shown in yellow stick format. Loop 3 (the second β-strand loop) and Loop 2 are both involved; residues K99, R102, R114, R116, R119, R131, R133, K134, R136, K142, K144 and R145 form a linear heparin binding site capable of accommodating a heparin dodecamer [26]. (C) The dimer of the CAN BMP antagonist gremlin (co-ordinates from 5AEJ.pdb). Here, the heparin binding residues are located largely along the second “finger”, as for sclerostin; in the dimer both copies of the heparin binding site are on the concave face. Residues K145, K147, K148, K167, K168, K169, K174 and R177 have been identified as forming the heparin binding site [20]. The mode of dimerisation and the location of the heparin binding site both differ from those of TGF-β1.

Figure 1. The TGF-β superfamily cystine knot fold, as typified by TGF-β1 (co-ordinates from 1KLC.pdb). Protein chains are shown in ribbon format: β-strands are blue, helices red, turns green; cystines are shown in yellow stick format. (A) TGF-β1 monomer showing the “hand” structures, with the cystine knot indicated by a green ellipse. (B) TGF-β1 dimer, the “wrist” of each hand is cupped in the other subunit. The view of the dimer is rotated by 90° with respect to the plane of 1A. The interchain disulphide bridge is visible in the centre of the structure.
Date
Source https://www.mdpi.com/1420-3049/22/5/713 Rider, C.C.; Mulloy, B. Heparin, Heparan Sulphate and the TGF-β Cytokine Superfamily. Molecules 2017, 22, 713. https://doi.org/10.3390/molecules22050713
Author Rider, C.C.; Mulloy, B.
This file, which was originally posted to an external website, has not yet been reviewed by an administrator or reviewer to confirm that the above license is valid. See Category:License review needed for further instructions.

© 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

Licensing

[edit]
w:en:Creative Commons
attribution
This file is licensed under the Creative Commons Attribution 4.0 International license.
You are free:
  • to share – to copy, distribute and transmit the work
  • to remix – to adapt the work
Under the following conditions:
  • attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.

File history

Click on a date/time to view the file as it appeared at that time.

Date/TimeThumbnailDimensionsUserComment
current20:27, 18 December 2024Thumbnail for version as of 20:27, 18 December 20241,437 × 923 (695 KB)Rasbak (talk | contribs){{Information |description=Figure 2. Heparin binding sites on TGF-β superfamily cytokines. Protein chains are shown as in Figure 1, and heparin binding site basic residues are shown in brown stick format. (A) The dimer of TGF-β1 (co-ordinates from 1KLC.pdb). Residues K25, R26, K31, K37, R94 and R97 form a discontinuous heparin binding site at the tips of the “fingers” [13]. (B) Sclerostin monomer (one of the NMR ensemble in 2K8P.pdb) with heparin-binding residues in brown. Cystine residues ar...

There are no pages that use this file.

File usage on other wikis

The following other wikis use this file:

Metadata