1B9P

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

1B9P の概要

• エントリーDOI: 10.2210/pdb1b9p/pdb
• NMR情報: BMRB: 4481
• 分子名称: PROTEIN (COLLAGEN ALPHA 1) (1 entity in total)
• 機能のキーワード: collagen facit xiv, heparin-binding site, nc1
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4020.76

構造登録者

Montserret, R.,Deleage, G.,Penin, F. (登録日: 1999-02-15, 公開日: 1999-02-25, 最終更新日: 2023-12-27)

主引用文献

Montserret, R.,Aubert-Foucher, E.,McLeish, M.J.,Hill, J.M.,Ficheux, D.,Jaquinod, M.,van der Rest, M.,Deleage, G.,Penin, F.
Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR.
Biochemistry, 38:6479-6488, 1999

PubMed Abstract: 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.

PubMed: 10350466
DOI: 10.1021/bi9900222

実験手法

SOLUTION NMR