PDBsum entry 1n11

Structural protein

PDB id: 1n11

Contents

Protein chain

404 a.a. *

Metals

_CL ×9

_BR

* Residue conservation analysis

PDB id:

1n11

Name:

Structural protein

Title:

D34 region of human ankyrin-r and linker

Structure:

Ankyrin. Chain: a. Fragment: d34 region. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ank-1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.319 R-free: 0.303

Authors:

P.Michaely,D.R.Tomchick,M.Machius,R.G.W.Anderson

Key ref:

P.Michaely et al. (2002). Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J, 21, 6387-6396. PubMed id: 12456646 DOI: 10.1093/emboj/cdf651

Date:

16-Oct-02 Release date: 11-Dec-02

Protein chain

P16157  (ANK1_HUMAN) -  Ankyrin-1 from Homo sapiens

Seq: 1881 a.a.

Struc: 404 a.a.

DOI no: 10.1093/emboj/cdf651

EMBO J 21:6387-6396 (2002)

PubMed id: 12456646

Crystal structure of a 12 ANK repeat stack from human ankyrinR.

P.Michaely, D.R.Tomchick, M.Machius, R.G.Anderson.

ABSTRACT

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.

Selected figure(s)

Figure 1.
Figure 1 Structure of the D34 region of ankyrinR. (A) Ankyrins typically are composed of four domains: an ANK repeat bearing, 'membrane-binding' domain, a central 'spectrin-binding' domain, a death domain (DD) and a C-terminal regulatory domain. The D34 region of ankyrinR contains ANK repeats 13−24 and a short portion of the spectrin-binding domain. Cylinders indicate the positions of the two helical segments in each repeat. Amino acids are given as one-letter code, where indicates a non-polar residue. Position numbering within repeats is based upon the exon−intron boundaries of the ank1 gene. The amino acid sequence of the D34 region is shown, with the repeat designation on the left and the amino acid number on the right of the sequence block. (B) Stereo view of D34. Individual repeats are rainbow colored such that repeat 13 is red and repeat 24 is violet. (C) Surface labels are given for the repeat stack. The bottom image is rotated 90° relative to the top image.

Figure 6.
Figure 6 Membrane-binding domain. (A) A stereo view of a model of the membrane-binding domain viewed along the spiral axis with the C-terminus closest to the viewer. Repeats are rainbow colored such that repeat 1 is red and repeat 24 is violet. (B) An extension of the D34−CDB3 model to include all 24 repeats of the membrane-binding domain and all four subunits of the CDB3 tetramer. The membrane-binding domain is shown as a green ribbon, while the four subunits of the tetramer are shown as red, blue, cyan and pink ribbons. The D34 region of the membrane-binding domain interacts with the red subunit.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2002, 21, 6387-6396) copyright 2002.

Figures were selected by the author.