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2z4f
From Proteopedia
(New page: 200px<br /> <applet load="2z4f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2z4f" /> '''Solution structure of the Discoidin Domain ...) |
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| - | [[Image:2z4f.gif|left|200px]]<br /> | + | [[Image:2z4f.gif|left|200px]]<br /><applet load="2z4f" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2z4f" size=" | + | |
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'''Solution structure of the Discoidin Domain of DDR2'''<br /> | '''Solution structure of the Discoidin Domain of DDR2'''<br /> | ||
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==Overview== | ==Overview== | ||
Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase, activated by the binding of its discoidin (DS) domain to fibrillar, collagen. Here, we have determined the NMR structure of the DS domain in, DDR2 (DDR2-DS domain), and identified the binding site to fibrillar, collagen by transferred cross-saturation experiments. The DDR2-DS domain, structure adopts a distorted jellyroll fold, consisting of eight, beta-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The, surface profile of the collagen-binding site suggests that the DDR2-DS, domain recognizes specific sites on fibrillar collagen. This study, provides a molecular basis for the collagen-binding mode of the DDR2-DS, domain. | Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase, activated by the binding of its discoidin (DS) domain to fibrillar, collagen. Here, we have determined the NMR structure of the DS domain in, DDR2 (DDR2-DS domain), and identified the binding site to fibrillar, collagen by transferred cross-saturation experiments. The DDR2-DS domain, structure adopts a distorted jellyroll fold, consisting of eight, beta-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The, surface profile of the collagen-binding site suggests that the DDR2-DS, domain recognizes specific sites on fibrillar collagen. This study, provides a molecular basis for the collagen-binding mode of the DDR2-DS, domain. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Wernicke-Korsakoff syndrome, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606781 606781]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2Z4F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http:// | + | 2Z4F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z4F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:51:44 2008'' |
Revision as of 10:51, 23 January 2008
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Solution structure of the Discoidin Domain of DDR2
Overview
Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase, activated by the binding of its discoidin (DS) domain to fibrillar, collagen. Here, we have determined the NMR structure of the DS domain in, DDR2 (DDR2-DS domain), and identified the binding site to fibrillar, collagen by transferred cross-saturation experiments. The DDR2-DS domain, structure adopts a distorted jellyroll fold, consisting of eight, beta-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The, surface profile of the collagen-binding site suggests that the DDR2-DS, domain recognizes specific sites on fibrillar collagen. This study, provides a molecular basis for the collagen-binding mode of the DDR2-DS, domain.
About this Structure
2Z4F is a Single protein structure of sequence from Homo sapiens. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.
Reference
Structural basis of the collagen-binding mode of discoidin domain receptor 2., Ichikawa O, Osawa M, Nishida N, Goshima N, Nomura N, Shimada I, EMBO J. 2007 Aug 16;. PMID:17703188
Page seeded by OCA on Wed Jan 23 12:51:44 2008
