1UAP
NMR structure of the NTR domain from human PCOLCE1
Summary for 1UAP
| Entry DOI | 10.2210/pdb1uap/pdb |
| Descriptor | Procollagen C-proteinase enhancer protein (1 entity in total) |
| Functional Keywords | beta barrel, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: Q15113 |
| Total number of polymer chains | 1 |
| Total formula weight | 16586.18 |
| Authors | Liepinsh, E.,Banyai, L.,Pintacuda, G.,Trexler, M.,Patthy, L.,Otting, G. (deposition date: 2003-03-14, release date: 2003-07-15, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 12670942DOI: 10.1074/jbc.M302734200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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