1n11
From Proteopedia
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|PDB= 1n11 |SIZE=350|CAPTION= <scene name='initialview01'>1n11</scene>, resolution 2.70Å | |PDB= 1n11 |SIZE=350|CAPTION= <scene name='initialview01'>1n11</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> | + | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ank-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ank-1 ([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=1n11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n11 OCA], [http://www.ebi.ac.uk/pdbsum/1n11 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n11 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. The N-terminal, 'membrane-binding' domain of ankyrins contains 24 ANK repeats and mediates most binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. Here we report the crystal structure of a human ankyrinR construct containing ANK repeats 13-24 and a portion of the spectrin-binding domain. The ANK repeats are observed to form a contiguous spiral stack with which the spectrin-binding domain fragment associates as an extended strand. The structural information has been used to construct models of all 24 repeats of the membrane-binding domain as well as the interactions of the repeats with the Cl/HCO(3) anion exchanger and clathrin. These models, together with available binding studies, suggest that ion transporters such as the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. | Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. The N-terminal, 'membrane-binding' domain of ankyrins contains 24 ANK repeats and mediates most binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. Here we report the crystal structure of a human ankyrinR construct containing ANK repeats 13-24 and a portion of the spectrin-binding domain. The ANK repeats are observed to form a contiguous spiral stack with which the spectrin-binding domain fragment associates as an extended strand. The structural information has been used to construct models of all 24 repeats of the membrane-binding domain as well as the interactions of the repeats with the Cl/HCO(3) anion exchanger and clathrin. These models, together with available binding studies, suggest that ion transporters such as the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Chondrocalcinosis 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605145 605145]], Craniometaphyseal dysplasia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605145 605145]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Michaely, P.]] | [[Category: Michaely, P.]] | ||
[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
| - | [[Category: BR]] | ||
| - | [[Category: CL]] | ||
[[Category: anion exchanger]] | [[Category: anion exchanger]] | ||
[[Category: ankyrin]] | [[Category: ankyrin]] | ||
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[[Category: clathrin]] | [[Category: clathrin]] | ||
| - | ''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 22:23:52 2008'' |
Revision as of 19:23, 30 March 2008
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| , resolution 2.70Å | |||||||
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| Ligands: | , | ||||||
| Gene: | ank-1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
D34 REGION OF HUMAN ANKYRIN-R AND LINKER
Overview
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. The N-terminal, 'membrane-binding' domain of ankyrins contains 24 ANK repeats and mediates most binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. Here we report the crystal structure of a human ankyrinR construct containing ANK repeats 13-24 and a portion of the spectrin-binding domain. The ANK repeats are observed to form a contiguous spiral stack with which the spectrin-binding domain fragment associates as an extended strand. The structural information has been used to construct models of all 24 repeats of the membrane-binding domain as well as the interactions of the repeats with the Cl/HCO(3) anion exchanger and clathrin. These models, together with available binding studies, suggest that ion transporters such as the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
About this Structure
1N11 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a 12 ANK repeat stack from human ankyrinR., Michaely P, Tomchick DR, Machius M, Anderson RG, EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
Page seeded by OCA on Sun Mar 30 22:23:52 2008
