1lsl

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|PDB= 1lsl |SIZE=350|CAPTION= <scene name='initialview01'>1lsl</scene>, resolution 1.90&Aring;
|PDB= 1lsl |SIZE=350|CAPTION= <scene name='initialview01'>1lsl</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene> and <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>
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|LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= THBS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= THBS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsl OCA], [http://www.ebi.ac.uk/pdbsum/1lsl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lsl RCSB]</span>
}}
}}
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==Overview==
==Overview==
Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases. The crystal structure of the TSRs reported in this article reveals a novel, antiparallel, three-stranded fold that consists of alternating stacked layers of tryptophan and arginine residues from respective strands, capped by disulfide bonds on each end. The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands. This is the first high-resolution crystal structure of a TSR domain that provides a prototypic architecture for structural and functional exploration of the diverse members of the TSR superfamily.
Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases. The crystal structure of the TSRs reported in this article reveals a novel, antiparallel, three-stranded fold that consists of alternating stacked layers of tryptophan and arginine residues from respective strands, capped by disulfide bonds on each end. The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands. This is the first high-resolution crystal structure of a TSR domain that provides a prototypic architecture for structural and functional exploration of the diverse members of the TSR superfamily.
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==Disease==
 
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Known disease associated with this structure: Sudden infant death with dysgenesis of the testes syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604714 604714]]
 
==About this Structure==
==About this Structure==
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[[Category: Wang, J H.]]
[[Category: Wang, J H.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
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[[Category: FUC]]
 
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[[Category: FUL]]
 
[[Category: tsp-1]]
[[Category: tsp-1]]
[[Category: tsr]]
[[Category: tsr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:48 2008''

Revision as of 19:06, 30 March 2008


PDB ID 1lsl

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: ,
Gene: THBS1 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Thrombospondin-1 Type 1 Repeats


Overview

Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases. The crystal structure of the TSRs reported in this article reveals a novel, antiparallel, three-stranded fold that consists of alternating stacked layers of tryptophan and arginine residues from respective strands, capped by disulfide bonds on each end. The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands. This is the first high-resolution crystal structure of a TSR domain that provides a prototypic architecture for structural and functional exploration of the diverse members of the TSR superfamily.

About this Structure

1LSL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication., Tan K, Duquette M, Liu JH, Dong Y, Zhang R, Joachimiak A, Lawler J, Wang JH, J Cell Biol. 2002 Oct 28;159(2):373-82. Epub 2002 Oct 21. PMID:12391027

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