1b9p: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1b9p.jpg|left|200px]] | [[Image:1b9p.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1b9p", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1b9p| PDB=1b9p | SCENE= }} | |||
}} | |||
'''NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV''' | '''NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1B9P is a [[Single protein]] structure | 1B9P is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9P OCA]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 24: | ||
[[Category: Montserret, R.]] | [[Category: Montserret, R.]] | ||
[[Category: Penin, F.]] | [[Category: Penin, F.]] | ||
[[Category: | [[Category: Collagen facit xiv]] | ||
[[Category: | [[Category: Heparin-binding site]] | ||
[[Category: | [[Category: Nc1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:14:55 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:14, 2 May 2008
NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV
OverviewOverview
Type XIV collagen, a fibril-associated collagen with interrupted triple helices (FACIT), interacts with the surrounding extracellular matrix and/or with cells via its binding to glycosaminoglycans (GAGs). To further characterize such interactions in the NC1 domain of chicken collagen XIV, we identified amino acids essential for heparin binding by affinity chromatography analysis after proteolytic digestion of the synthetic peptide NC1(84-116). The 3D structure of this peptide was then obtained using circular dichroism and NMR. The NC1(84-116) peptide appeared poorly structured in water, but the stabilization of its conformation by the interaction with hydrophobic surfaces or by using cosolvents (TFE, SDS) revealed a high propensity to adopt an alpha-helical folding. A 3D structure model of NC1(84-116), calculated from NMR data recorded in a TFE/water mixture, showed that the NC1-heparin binding site forms a amphipathic alpha-helix exhibiting a twisted basic groove. It is structurally similar to the consensus spatial alpha-helix model of heparin-binding [Margalit et al. (1993) J. Biol. Chem. 268, 19228-19231], except that the GAG binding domain of NC1 may be extended over 18 residues, that is, the NC1(94-111) segment. In addition, the formation of a hydrophobic groove upon helix formation suggests the contribution of additional sequences to ensure the stability of the GAG-binding domain. Overall the NC1(84-116) model exhibits a nativelike conformation which presents suitably oriented residues for the interaction with a specific GAG.
About this StructureAbout this Structure
1B9P is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR., Montserret R, Aubert-Foucher E, McLeish MJ, Hill JM, Ficheux D, Jaquinod M, van der Rest M, Deleage G, Penin F, Biochemistry. 1999 May 18;38(20):6479-88. PMID:10350466 Page seeded by OCA on Fri May 2 11:14:55 2008