1xku
From Proteopedia
(New page: 200px<br /><applet load="1xku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xku, resolution 2.15Å" /> '''Crystal structure of...) |
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| - | [[Image:1xku.gif|left|200px]]<br /><applet load="1xku" size=" | + | [[Image:1xku.gif|left|200px]]<br /><applet load="1xku" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xku, resolution 2.15Å" /> | caption="1xku, resolution 2.15Å" /> | ||
'''Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan'''<br /> | '''Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Decorin is a ubiquitous extracellular matrix proteoglycan with a variety | + | Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core of decorin, the best characterized member of the SLRP family. Each monomer adopts the curved solenoid fold characteristic of LRR domains, with a parallel beta-sheet on the inside interwoven with loops containing short segments of beta-strands, 3(10) helices, and polyproline II helices on the outside. Two main features are unique to this structure. First, decorin dimerizes through the concave surfaces of the LRR domains, which have been implicated previously in protein-ligand interactions. The amount of surface buried in this dimer rivals the buried surfaces of some of the highest-affinity macromolecular complexes reported to date. Second, the C-terminal region adopts an unusual capping motif that involves a laterally extended LRR and a disulfide bond. This motif seems to be unique to SLRPs and has not been observed in any other LRR protein structure to date. Possible implications of these features for decorin ligand binding and SLRP function are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1XKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bella, J.]] | [[Category: Bella, J.]] | ||
| - | [[Category: Bergmann, E | + | [[Category: Bergmann, E M.]] |
| - | [[Category: Bishop, P | + | [[Category: Bishop, P N.]] |
| - | [[Category: Dodd, C | + | [[Category: Dodd, C M.]] |
| - | [[Category: McEwan, P | + | [[Category: McEwan, P A.]] |
| - | [[Category: Scott, P | + | [[Category: Scott, P G.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: TRS]] | [[Category: TRS]] | ||
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[[Category: proteoglycan]] | [[Category: proteoglycan]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:52 2008'' |
Revision as of 13:55, 21 February 2008
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Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
Overview
Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core of decorin, the best characterized member of the SLRP family. Each monomer adopts the curved solenoid fold characteristic of LRR domains, with a parallel beta-sheet on the inside interwoven with loops containing short segments of beta-strands, 3(10) helices, and polyproline II helices on the outside. Two main features are unique to this structure. First, decorin dimerizes through the concave surfaces of the LRR domains, which have been implicated previously in protein-ligand interactions. The amount of surface buried in this dimer rivals the buried surfaces of some of the highest-affinity macromolecular complexes reported to date. Second, the C-terminal region adopts an unusual capping motif that involves a laterally extended LRR and a disulfide bond. This motif seems to be unique to SLRPs and has not been observed in any other LRR protein structure to date. Possible implications of these features for decorin ligand binding and SLRP function are discussed.
About this Structure
1XKU is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan., Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J, Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15633-8. Epub 2004 Oct 22. PMID:15501918
Page seeded by OCA on Thu Feb 21 15:55:52 2008
Categories: Bos taurus | Single protein | Bella, J. | Bergmann, E M. | Bishop, P N. | Dodd, C M. | McEwan, P A. | Scott, P G. | NAG | TRS | Leucine-rich repeat | Proteoglycan
