PDBsum entry 2gle

Protein binding

PDB id: 2gle

Contents

Protein chain

74 a.a. *

* Residue conservation analysis

PDB id:

2gle

Name:

Protein binding

Title:

Solution structure of neurabin sam domain

Structure:

Neurabin-1. Chain: a. Fragment: sam domain (residues 986-1056). Synonym: neurabin-i, neural tissue-specific f-actin-binding protein i, protein phosphatase 1 regulatory subunit 9a, p180, pp1bp175. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

T.Ju,J.Hudak,W.Peti

Key ref:

T.Ju et al. (2007). Structural characterization of the neurabin sterile alpha motif domain. Proteins, 69, 192-198. PubMed id: 17600833 DOI: 10.1002/prot.21513

Date:

04-Apr-06 Release date: 13-Mar-07

Protein chain

O35867  (NEB1_RAT) -  Neurabin-1 from Rattus norvegicus

Seq: 1095 a.a.

Struc: 74 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.21513

Proteins 69:192-198 (2007)

PubMed id: 17600833

Structural characterization of the neurabin sterile alpha motif domain.

T.Ju, M.J.Ragusa, J.Hudak, A.C.Nairn, W.Peti.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. A, Domain structure of spinophilin (top) and neurabin (bottom). Sequence identity between the domains is annotated in the figure. B, Primary sequence alignment of the neurabin SAM and shank3 SAM domains. The zinc binding residues in shank3 and the corresponding residues in neurabin are highlighted by boxes (see text). The shank3 (M1803E) mutation that is necessary to achieve high enough protein solubility and reduced aggregation is underlined. Secondary structure for the neurabin SAM domain is included above the sequence alignment.

Figure 2.
Figure 2. A, Stereo view of the bundle of 20 energy-minimized CYANA conformers representing the structure of neurabin[986-1056] (PDB ID 2GLE). The superposition is the best fit of the backbone atoms N, C^ , C of residues 4-70. Side chains with low local RMSD (<0.7) within the bundle are shown in cyan. Side chains of residues with high local RMSD (>0.7) are shown in green. Backbones are shown in dark blue. Aromatic heavy side chains are colored in orange. The local RMSD of Trp7, Trp15, Tyr24, and Phe28 are 0.31, 0.11, 0.87, and 0.62, respectively. B, Electrostatic surface of the neurabin SAM domain (left) and 180° rotation around x-axes (right). Red represents negative charges and blue positive charges. C, Ribbon presentation of the closest conformer to the mean coordinates of the bundle of 20 conformers used to represent the NMR structure of the neurabin SAM (left) and the shank3 SAM domain (right). The regular secondary structure elements are identified.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 192-198) copyright 2007.