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1n11

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(New page: 200px<br /> <applet load="1n11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n11, resolution 2.70&Aring;" /> '''D34 REGION OF HUMAN...)
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'''D34 REGION OF HUMAN ANKYRIN-R AND LINKER'''<br />
'''D34 REGION OF HUMAN ANKYRIN-R AND LINKER'''<br />
==Overview==
==Overview==
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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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1N11 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BR and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N11 OCA].
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1N11 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N11 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Anderson, R.G.W.]]
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[[Category: Anderson, R G.W.]]
[[Category: Machius, M.]]
[[Category: Machius, M.]]
[[Category: Michaely, P.]]
[[Category: Michaely, P.]]
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[[Category: Tomchick, D.R.]]
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[[Category: Tomchick, D R.]]
[[Category: BR]]
[[Category: BR]]
[[Category: CL]]
[[Category: CL]]
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[[Category: clathrin]]
[[Category: clathrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:16:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:05 2008''

Revision as of 12:01, 21 February 2008


1n11, resolution 2.70Å

Drag the structure with the mouse to rotate

D34 REGION OF HUMAN ANKYRIN-R AND LINKER

Contents

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.

Disease

Known diseases associated with this structure: Chondrocalcinosis 2 OMIM:[605145], Craniometaphyseal dysplasia OMIM:[605145]

About this Structure

1N11 is a Single protein structure of sequence from Homo sapiens with and as ligands. 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

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