Crystallographic insight into collagen recognition by discoidin domain receptor 2.
Crystallographic insight into collagen recognition by discoidin domain receptor 2.
复制标题
DOI:
10.1016/j.str.2009.10.012
复制
发表时间:
2009-12-09
期刊:
影响因子:
--
通讯作者:
Hohenester E
中科院分区:
文献类型:
--
作者:
Carafoli F;Bihan D;Stathopoulos S;Konitsiotis AD;Kvansakul M;Farndale RW;Leitinger B;Hohenester E
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.
登录
查看更多内容
影响因子:
9.8
作者:
Bargal, Ruth;Cormier-Daire, Valerie;Raas-Rothschild, Annick
通讯作者:
Raas-Rothschild, Annick
影响因子:
4.8
作者:
Ikeda, K;Wang, LH;Lin, HC
通讯作者:
Lin, HC
影响因子:
64.5
作者:
Emsley, J;Knight, CG;Liddington, RC
通讯作者:
Liddington, RC
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
DOI:
10.1073/pnas.0808452105
发表时间:
2008-11-25
影响因子:
11.1
作者:
Hohenester, Erhard;Sasaki, Takako;Baechinger, Hans Peter
通讯作者:
Baechinger, Hans Peter