PDBsum entry 3kbu

Structural protein

PDB id: 3kbu

Contents

Protein chains

285 a.a. *

153 a.a. *

156 a.a. *

Metals

_HG ×8

* Residue conservation analysis

PDB id:

3kbu

Name:

Structural protein

Title:

Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (zu5-ank), emts derivative

Structure:

Spectrin beta chain, erythrocyte. Chain: a, b. Fragment: unp residues 1583-1906. Synonym: beta-i spectrin. Engineered: yes. Mutation: yes. Ankyrin-1. Chain: c, d. Fragment: unp residues 911-1068.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sptb, sptb1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ank, ank1.

Resolution:

2.75Å R-factor: 0.228 R-free: 0.277

Authors:

J.J.Ipsaro,A.Mondragon

Key ref:

J.J.Ipsaro and A.Mondragón (2010). Structural basis for spectrin recognition by ankyrin. Blood, 115, 4093-4101. PubMed id: 20101027

Date:

20-Oct-09 Release date: 02-Feb-10

Protein chains

P11277  (SPTB1_HUMAN) -  Spectrin beta chain, erythrocytic from Homo sapiens

Seq: 2137 a.a.

Struc: 285 a.a.*

Protein chain

P16157  (ANK1_HUMAN) -  Ankyrin-1 from Homo sapiens

Seq: 1881 a.a.

Struc: 153 a.a.

Protein chain

P16157  (ANK1_HUMAN) -  Ankyrin-1 from Homo sapiens

Seq: 1881 a.a.

Struc: 156 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Blood 115:4093-4101 (2010)

PubMed id: 20101027

Structural basis for spectrin recognition by ankyrin.

J.J.Ipsaro, A.Mondragón.

ABSTRACT

Maintenance of membrane integrity and organization in the metazoan cell is accomplished through intracellular tethering of membrane proteins to an extensive, flexible protein network. Spectrin, the principal component of this network, is anchored to membrane proteins through the adaptor protein ankyrin. To elucidate the atomic basis for this interaction, we determined a crystal structure of human betaI-spectrin repeats 13 to 15 in complex with the ZU5-ANK domain of human ankyrin R. The structure reveals the role of repeats 14 to 15 in binding, the electrostatic and hydrophobic contributions along the interface, and the necessity for a particular orientation of the spectrin repeats. Using structural and biochemical data as a guide, we characterized the individual proteins and their interactions by binding and thermal stability analyses. In addition to validating the structural model, these data provide insight into the nature of some mutations associated with cell morphology defects, including those found in human diseases such as hereditary spherocytosis and elliptocytosis. Finally, analysis of the ZU5 domain suggests it is a versatile protein-protein interaction module with distinct interaction surfaces. The structure represents not only the first of a spectrin fragment in complex with its binding partner, but also that of an intermolecular complex involving a ZU5 domain.