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1ux6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Thrombospondins (TSPs) are extracellular regulators of cell-matrix | + | Thrombospondins (TSPs) are extracellular regulators of cell-matrix interactions and cell phenotype. The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. The T3 repeats lack secondary structure and are organised around a core of calcium ions; two DxDxDGxxDxxD motifs per repeat each encapsulate two calcium ions in a novel arrangement. The CTD forms a lectin-like beta-sandwich and contains four strictly conserved calcium-binding sites. Disruption of the hairpin structure of T3 repeats 6 and 7 decreases protein secretion and stability. The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading. The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly. |
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adams, J | + | [[Category: Adams, J C.]] |
[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
[[Category: Kvansakul, M.]] | [[Category: Kvansakul, M.]] | ||
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[[Category: l-type lectin]] | [[Category: l-type lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:17 2008'' |
Revision as of 13:29, 21 February 2008
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STRUCTURE OF A THROMBOSPONDIN C-TERMINAL FRAGMENT REVEALS A NOVEL CALCIUM CORE IN THE TYPE 3 REPEATS
Contents |
Overview
Thrombospondins (TSPs) are extracellular regulators of cell-matrix interactions and cell phenotype. The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. The T3 repeats lack secondary structure and are organised around a core of calcium ions; two DxDxDGxxDxxD motifs per repeat each encapsulate two calcium ions in a novel arrangement. The CTD forms a lectin-like beta-sandwich and contains four strictly conserved calcium-binding sites. Disruption of the hairpin structure of T3 repeats 6 and 7 decreases protein secretion and stability. The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading. The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly.
Disease
Known disease associated with this structure: Sudden infant death with dysgenesis of the testes syndrome OMIM:[604714]
About this Structure
1UX6 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats., Kvansakul M, Adams JC, Hohenester E, EMBO J. 2004 Mar 24;23(6):1223-33. Epub 2004 Mar 11. PMID:15014436
Page seeded by OCA on Thu Feb 21 15:29:17 2008
