1lsl: Difference between revisions
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'''Crystal Structure of the Thrombospondin-1 Type 1 Repeats''' | '''Crystal Structure of the Thrombospondin-1 Type 1 Repeats''' | ||
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[[Category: Wang, J H.]] | [[Category: Wang, J H.]] | ||
[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
[[Category: | [[Category: Tsp-1]] | ||
[[Category: | [[Category: Tsr]] | ||
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Revision as of 21:14, 2 May 2008
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 Page seeded by OCA on Sat May 3 00:14:44 2008
