1s35
From Proteopedia
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|PDB= 1s35 |SIZE=350|CAPTION= <scene name='initialview01'>1s35</scene>, resolution 2.40Å | |PDB= 1s35 |SIZE=350|CAPTION= <scene name='initialview01'>1s35</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SPTB, SPTB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SPTB, SPTB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s35 OCA], [http://www.ebi.ac.uk/pdbsum/1s35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s35 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility. | Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Anemia, neonatal hemolytic, fatal and near-fatal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]], Elliptocytosis-3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]], Spherocytosis-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: MacDonald, R I.]] | [[Category: MacDonald, R I.]] | ||
[[Category: Mondragon, A.]] | [[Category: Mondragon, A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: 3-helix coiled-coil]] | [[Category: 3-helix coiled-coil]] | ||
[[Category: alpha helical linker region]] | [[Category: alpha helical linker region]] | ||
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[[Category: two repeats of spectrin]] | [[Category: two repeats of spectrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:41 2008'' |
Revision as of 20:36, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Gene: | SPTB, SPTB1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin
Overview
Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.
About this Structure
1S35 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural insights into the stability and flexibility of unusual erythroid spectrin repeats., Kusunoki H, MacDonald RI, Mondragon A, Structure. 2004 Apr;12(4):645-56. PMID:15062087
Page seeded by OCA on Sun Mar 30 23:36:41 2008
