1b9q: Difference between revisions

Revision as of 18:39, 30 June 2008

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File:1b9q.png

Template:STRUCTURE 1b9q

NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIVNMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV

Template:ABSTRACT PUBMED 10350466

About this StructureAbout this Structure

1B9Q is a Single protein structure. Full experimental 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

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-[[Image:1b9q.jpg|left|200px]]
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 {{STRUCTURE_1b9q|  PDB=1b9q  |  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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10350466}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10350466 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10350466}}
 ==About this Structure==
-B9Q is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9Q OCA].
+B9Q is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9Q OCA].
 ==Reference==
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 [[Category: Heparin-binding site]]
 [[Category: Nc1]]
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