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      Characterization by high-resolution crystal structure analysis of a triple-helix region of human collagen type III with potent cell adhesion activity

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          Abstract

          Collagen is one of the most abundant and important proteins in the human body. Human collagen type III (hCOL3A1) belongs to the fibril-forming collagens and is widely distributed in extensible connective tissue like skin, internal organs, or the vascular system. It plays key roles in wound healing, collagen fibrillogenesis, and normal cardiovascular development in human. The charged residues are considered to be an important characteristic of hCOL3A1, especially for collagen binding and recognition. Here we found that a triple helix fragment of hCOL3A1, Gly489-Gly510, contained multiple charged residues, as well as representative Glu-Lys-Gly and Glu-Arg-Gly charged triplets. We solved the crystal structure of this new fragment to a high-resolution of 1.50 Å and identified some important conformations of this new triple-helix region, including strong hydrogen bonds in interchain and interhelical interactions in addition to obvious flexible bending for the triple helix. We also found that the synthetic collagen peptides around this region exhibited potent activities through integrin-mediated peptide-membrane interaction. We then developed a method to produce a recombinant protein consisting of 16 tandem repeats of the triple-helix fragment of hCOL3A1 with strong activity without cytotoxicity. These results provide a strong base for further functional studies of human collagen type III and the method developed in this study can be applied to produce hCOL3A1-derived proteins or other tandem-repeat proteins with membrane adhesion activity.

          Highlights

          • •

            hCOL3A1 plays important roles in wound healing and collagen fibrillogenesis.

          • •

            We solved crystal structure of hCOL3A1's triple-helix region G489-G510 at 1.5 Å.

          • •

            Peptides overlapping G489-G510 exhibited potent cell-adhesion activity.

          • •

            T16 protein containing tandem-repeated peptides is more effective than peptides.

          • •

            This study provides detail structural basis of hCOL3A1 related to its function.

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          Automated structure solution with the PHENIX suite.

          Peter H. Zwart, Pavel Afonine, Ralf W. Grosse-Kunstleve … (2008)
          Significant time and effort are often required to solve and complete a macromolecular crystal structure. The development of automated computational methods for the analysis, solution, and completion of crystallographic structures has the potential to produce minimally biased models in a short time without the need for manual intervention. The PHENIX software suite is a highly automated system for macromolecular structure determination that can rapidly arrive at an initial partial model of a structure without significant human intervention, given moderate resolution, and good quality data. This achievement has been made possible by the development of new algorithms for structure determination, maximum-likelihood molecular replacement (PHASER), heavy-atom search (HySS), template- and pattern-based automated model-building (RESOLVE, TEXTAL), automated macromolecular refinement (phenix. refine), and iterative model-building, density modification and refinement that can operate at moderate resolution (RESOLVE, AutoBuild). These algorithms are based on a highly integrated and comprehensive set of crystallographic libraries that have been built and made available to the community. The algorithms are tightly linked and made easily accessible to users through the PHENIX Wizards and the PHENIX GUI.
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            Collagens.

            R Hahn, Marion K. Gordon (2009)
            The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three alpha chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are non-glycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.
            Article 0 comments Cited 110 times – based on 0 reviews     Review now
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              The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens.

              P R Peachey, Danny S Tuckwell, R FARNDALE … (2000)
              We have previously assigned an integrin alpha(2)beta(1)-recognition site in collagen I to the sequence, GFOGERGVEGPOGPA (O = Hyp), corresponding to residues 502-516 of the alpha(1)(I) chain and located in the fragment alpha(1)(I)CB3 (Knight, C. G., Morton, L. F., Onley, D. J., Peachey, A. R., Messent, A. J., Smethurst, P. A., Tuckwell, D. S., Farndale, R. W., and Barnes, M. J. (1998) J. Biol. Chem. 273, 33287-33294). In this study, we show that recognition is entirely contained within the six-residue sequence GFOGER. This sequence, when in triple-helical conformation, readily supports alpha(2)beta(1)-dependent cell adhesion and exhibits divalent cation-dependent binding of isolated alpha(2)beta(1) and recombinant alpha(2) A-domain, being at least as active as the parent collagen. Replacement of E by D causes loss of recognition. The same sequence binds integrin alpha(1) A-domain and supports integrin alpha(1)beta(1)-mediated cell adhesion. Triple-helical GFOGER completely inhibits alpha(2) A-domain binding to collagens I and IV and alpha(2)beta(1)-dependent adhesion of platelets and HT 1080 cells to these collagens. It also fully inhibits alpha(1) A-domain binding to collagen I and strongly inhibits alpha(1)beta(1)-mediated adhesion of Rugli cells to this collagen but has little effect on either alpha1 A-domain binding or adhesion of Rugli cells to collagen IV. We conclude that the sequence GFOGER represents a high-affinity binding site in collagens I and IV for alpha(2)beta(1) and in collagen I for alpha(1)beta(1). Other high-affinity sites in collagen IV mediate its recognition of alpha(1)beta(1).
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                Author and article information

                Contributors
                Rongguang Zhang
                Lu Lu
                Shibo Jiang
                Journal
                Journal ID (nlm-ta): Biochem Biophys Res Commun
                Journal ID (iso-abbrev): Biochem. Biophys. Res. Commun
                Title: Biochemical and Biophysical Research Communications
                Publisher: Elsevier
                ISSN (Print): 0006-291X
                ISSN (Electronic): 1090-2104
                Publication date PMC-release: 11 December 2018
                Publication date (Print): 22 January 2019
                Publication date (Electronic): 11 December 2018
                Volume: 508
                Issue: 4
                Pages: 1018-1023
                Affiliations
                [a ]Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan-Jinbo Joint Research Center, Fudan University, Shanghai, 200302, China
                [b ]National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China
                [c ]National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Science, Chinese Academy of Sciences, Shanghai, China
                Author notes
                [∗ ]Corresponding author.National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. rzhang@ 123456ibp.ac.cn
                [∗∗ ]Corresponding author. Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan-Jinbo Joint Research Center, Fudan University, Shanghai, 200302, China. lul@ 123456fudan.edu.cn
                [∗∗∗ ]Corresponding author. Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences, Fudan-Jinbo Joint Research Center, Fudan University, Shanghai, 200302, China. shibojiang@ 123456fudan.edu.cn
                [1]

                These authors contributed equally to this work.

                Article
                Publisher ID: S0006-291X(18)32663-9
                DOI: 10.1016/j.bbrc.2018.12.018
                PMC ID: 7092849
                PubMed ID: 30545625
                SO-VID: 3cf91482-0099-4b87-9383-b11122e62d11
                Copyright © © 2018 Elsevier Inc. All rights reserved.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 19 November 2018
                Date accepted : 4 December 2018
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Keywords: human collagen type iii peptide,triple-helix region,crystal structure,cell adhesion
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: human collagen type iii peptide, triple-helix region, crystal structure, cell adhesion

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