Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Aug 16;7:8304. doi: 10.1038/s41598-017-08588-5

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

The identification of acrolein-modified residues in SP-A. (A) Nano-LC/MALDI-TOF MS/MS analysis of peptides obtained from the trypsin digestion of acrolein-modified hSP-A. Trypsin digested acrolein-modified SP-A was subjected to Nano-LC/MALDI-TOF MS/MS analysis and identified by using MASCOT Daemon. Acrolein-modified residues are shown in red. (Upper) The MS/MS analysis of non-reduced acrolein-modified SP-A. (Lower) The MS/MS analysis of NaBH_4-reduced acrolein-modified SP-A. (B) The amino acid sequence of hSP-A. Acrolein-modified residues are shown in red, and the double-loop structure is indicated by the blue underlined text. (C) The structural organisation of human SP-A. SP-A is conceptually divided into a signal peptide, N-terminal, collagen-like neck and CRD domain. The double-loop structure in the CRD domain is shown in blue (long loop residues: 219–226 and short loop residues: 191–197). Green corresponds to residues 104–248, which are shown in the crystal structure in (D). (D) A homology model of the hSP-A neck and CRD domains (residues: 104–248) based on the crystal structure of rat SP-A (PDB ID: 1R13). The model was constructed using SWISS-MODEL³⁷. The protein backbone is shown in green, the double-loop structure in the CRD domain is shown in blue, and acrolein-modified residues are highlighted in red.