1lsl: Difference between revisions

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[[Image:1lsl.jpg|left|200px]]
{{Seed}}
[[Image:1lsl.png|left|200px]]


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{{STRUCTURE_1lsl|  PDB=1lsl  |  SCENE=  }}  
{{STRUCTURE_1lsl|  PDB=1lsl  |  SCENE=  }}  


'''Crystal Structure of the Thrombospondin-1 Type 1 Repeats'''
===Crystal Structure of the Thrombospondin-1 Type 1 Repeats===




==Overview==
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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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{{ABSTRACT_PUBMED_12391027}}


==About this Structure==
==About this Structure==
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[[Category: Tsp-1]]
[[Category: Tsp-1]]
[[Category: Tsr]]
[[Category: Tsr]]
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Revision as of 19:02, 2 July 2008

File:1lsl.png

Template:STRUCTURE 1lsl

Crystal Structure of the Thrombospondin-1 Type 1 Repeats

Template:ABSTRACT PUBMED 12391027

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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