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1ux6
From Proteopedia
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|PDB= 1ux6 |SIZE=350|CAPTION= <scene name='initialview01'>1ux6</scene>, resolution 1.90Å | |PDB= 1ux6 |SIZE=350|CAPTION= <scene name='initialview01'>1ux6</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ux6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux6 OCA], [http://www.ebi.ac.uk/pdbsum/1ux6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ux6 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604714 604714]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
[[Category: Kvansakul, M.]] | [[Category: Kvansakul, M.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
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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 Mon Mar 31 00:16:34 2008'' |
Revision as of 21:16, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A THROMBOSPONDIN C-TERMINAL FRAGMENT REVEALS A NOVEL CALCIUM CORE IN THE TYPE 3 REPEATS
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.
About this Structure
1UX6 is a Single protein structure of sequence from Homo sapiens. 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 Mon Mar 31 00:16:34 2008
