1YO8

Structure of the C-terminal domain of human thrombospondin-2

Summary for 1YO8

• Entry DOI: 10.2210/pdb1yo8/pdb
• Descriptor: thrombospondin-2, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: egf; ca(2+)-binding domains; lectin domain; disulfide, cell adhesion
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 73528.07

Authors

Carlson, C.B.,Bernstein, D.A.,Annis, D.S.,Misenheimer, T.M.,Hannah, B.A.,Mosher, D.F.,Keck, J.L. (deposition date: 2005-01-26, release date: 2005-09-27, Last modification date: 2020-07-29)

Primary citation

Carlson, C.B.,Bernstein, D.A.,Annis, D.S.,Misenheimer, T.M.,Hannah, B.L.,Mosher, D.F.,Keck, J.L.
Structure of the calcium-rich signature domain of human thrombospondin-2
Nat.Struct.Mol.Biol., 12:910-914, 2005

PubMed Abstract: Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.

PubMed: 16186819
DOI: 10.1038/nsmb997

Experimental method

X-RAY DIFFRACTION (2.6 Å)