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2v53
From Proteopedia
| 2v53, resolution 3.20Å () | |||||
|---|---|---|---|---|---|
| Sites: | , , and | ||||
| Ligands: | , , | ||||
| Non-Standard Residues: | |||||
| Related: | 1nub, 1bmo, 1sra | ||||
| |||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||
| Coordinates: | save as pdb, mmCIF, xml | ||||
CRYSTAL STRUCTURE OF A SPARC-COLLAGEN COMPLEX
Protein interactions with the collagen triple helix play a critical role in collagen fibril formation, cell adhesion, and signaling. However, structural insight into sequence-specific collagen recognition is limited to an integrin-peptide complex. A GVMGFO motif in fibrillar collagens (O denotes 4-hydroxyproline) binds 3 unrelated proteins: von Willebrand factor (VWF), discoidin domain receptor 2 (DDR2), and the extracellular matrix protein SPARC/osteonectin/BM-40. We report the crystal structure at 3.2 A resolution of human SPARC bound to a triple-helical 33-residue peptide harboring the promiscuous GVMGFO motif. SPARC recognizes the GVMGFO motifs of the middle and trailing collagen chains, burying a total of 720 A(2) of solvent-accessible collagen surface. SPARC binding does not distort the canonical triple helix of the collagen peptide. In contrast, a critical loop in SPARC is substantially remodelled upon collagen binding, creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain ("Phe pocket"). This highly restrictive specificity pocket is shared with the collagen-binding integrin I-domains but differs strikingly from the shallow collagen-binding grooves of the platelet receptor glycoprotein VI and microbial adhesins. We speculate that binding of the GVMGFO motif to VWF and DDR2 also results in structural changes and the formation of a Phe pocket.
Structural basis of sequence-specific collagen recognition by SPARC., Hohenester E, Sasaki T, Giudici C, Farndale RW, Bachinger HP, Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18273-7. Epub 2008 Nov 14. PMID:19011090
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2v53 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Hohenester E, Sasaki T, Giudici C, Farndale RW, Bachinger HP. Structural basis of sequence-specific collagen recognition by SPARC. Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18273-7. Epub 2008 Nov 14. PMID:19011090 doi:0808452105
- Sasaki T, Hohenester E, Gohring W, Timpl R. Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin. EMBO J. 1998 Mar 16;17(6):1625-34. PMID:9501084 doi:10.1093/emboj/17.6.1625
