2WUH

Crystal structure of the DDR2 discoidin domain bound to a triple- helical collagen peptide

Summary for 2WUH

• Entry DOI: 10.2210/pdb2wuh/pdb
• Descriptor: DISCOIDIN DOMAIN RECEPTOR 2, COLLAGEN PEPTIDE (3 entities in total)
• Functional Keywords: receptor-peptide complex, transferase, nucleotide-binding, tyrosine-protein kinase, receptor/peptide
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: Q16832
• Total number of polymer chains: 4
• Total formula weight: 28010.18

Authors

Carafoli, F.,Bihan, D.,Stathopoulos, S.,Konitsiotis, A.D.,Kvansakul, M.,Farndale, R.W.,Leitinger, B.,Hohenester, E. (deposition date: 2009-10-05, release date: 2009-12-29, Last modification date: 2023-12-20)

Primary citation

Carafoli, F.,Bihan, D.,Stathopoulos, S.,Konitsiotis, A.D.,Kvansakul, M.,Farndale, R.W.,Leitinger, B.,Hohenester, E.
Crystallographic Insight Into Collagen Recognition by Discoidin Domain Receptor 2
Structure, 17:1573-, 2009

PubMed Abstract: The discoidin domain receptors, DDR1 and DDR2, are widely expressed receptor tyrosine kinases that are activated by triple-helical collagen. They control important aspects of cell behavior and are dysregulated in several human diseases. The major DDR2-binding site in collagens I-III is a GVMGFO motif (O is hydroxyproline) that also binds the matricellular protein SPARC. We have determined the crystal structure of the discoidin domain of human DDR2 bound to a triple-helical collagen peptide. The GVMGFO motifs of two collagen chains are recognized by an amphiphilic pocket delimited by a functionally critical tryptophan residue and a buried salt bridge. Collagen binding results in structural changes of DDR2 surface loops that may be linked to the process of receptor activation. A comparison of the GVMGFO-binding sites of DDR2 and SPARC reveals a striking case of convergent evolution in collagen recognition.

PubMed: 20004161
DOI: 10.1016/J.STR.2009.10.012

Experimental method

X-RAY DIFFRACTION (1.6 Å)