1UAP

NMR structure of the NTR domain from human PCOLCE1

1UAP の概要

• エントリーDOI: 10.2210/pdb1uap/pdb
• 分子名称: Procollagen C-proteinase enhancer protein (1 entity in total)
• 機能のキーワード: beta barrel, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: Q15113
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16586.18

構造登録者

Liepinsh, E.,Banyai, L.,Pintacuda, G.,Trexler, M.,Patthy, L.,Otting, G. (登録日: 2003-03-14, 公開日: 2003-07-15, 最終更新日: 2024-11-20)

主引用文献

Liepinsh, E.,Banyai, L.,Pintacuda, G.,Trexler, M.,Patthy, L.,Otting, G.
NMR Structure of the Netrin-like Domain (NTR) of Human Type I Procollagen C-Proteinase Enhancer Defines Structural Consensus of NTR Domains and Assesses Potential Proteinase Inhibitory Activity and Ligand Binding.
J.Biol.Chem., 278:25982-25989, 2003

PubMed Abstract: Procollagen C-proteinase enhancer (PCOLCE) proteins are extracellular matrix proteins that enhance the activities of procollagen C-proteinases by binding to the C-propeptide of procollagen I. PCOLCE proteins are built of three structural modules, consisting of two CUB domains followed by a C-terminal netrin-like (NTR) domain. While the enhancement of proteinase activity can be ascribed solely to the CUB domains, sequence homology of the NTR domain with tissue inhibitors of metalloproteinases suggest proteinase inhibitory activity for the NTR domain. Here we present the three-dimensional structure of the NTR domain of human PCOLCE1 as the first example of a structural domain with the canonical features of an NTR module. The structure rules out a binding mode to metalloproteinases similar to that of tissue inhibitors of metalloproteinases but suggests possible inhibitory function toward specific serine proteinases. Sequence conservation between 13 PCOLCE proteins from different organisms suggests a conserved binding surface for other protein partners.

PubMed: 12670942
DOI: 10.1074/jbc.M302734200

実験手法

SOLUTION NMR