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1lsl

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(New page: 200px<br /> <applet load="1lsl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lsl, resolution 1.90&Aring;" /> '''Crystal Structure o...)
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Revision as of 15:57, 12 November 2007

Image:1lsl.gif

1lsl, resolution 1.90Å

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Crystal Structure of the Thrombospondin-1 Type 1 Repeats

Contents

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.

Disease

Known disease associated with this structure: Sudden infant death with dysgenesis of the testes syndrome OMIM:[604714]

About this Structure

1LSL is a Single protein structure of sequence from Homo sapiens with FUL and FUC as ligands. 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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