PDBsum entry 2rq1

Membrane protein

PDB id: 2rq1

Contents

Protein chain

109 a.a. *

* Residue conservation analysis

PDB id:

2rq1

Name:

Membrane protein

Title:

Solution structure of the 4.1r ferm alpha lobe domain

Structure:

Protein 4.1. Chain: a. Fragment: 4.1r_ferm_alpha-lobe_domain, unp residues 292-396. Synonym: band 4.1, p4.1, epb4.1, 4.1r. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: epb41, e41p. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

H.Kusunoki,T.Kohno

Key ref:

H.Kusunoki and T.Kohno (2009). Solution structure and glycophorin C binding studies of the protein 4.1R FERM alpha-lobe domain. Proteins, 76, 255-260. PubMed id: 19338061 DOI: 10.1002/prot.22405

Date:

09-Jan-09 Release date: 14-Apr-09

Protein chain

P11171  (41_HUMAN) -  Protein 4.1 from Homo sapiens

Seq: 864 a.a.

Struc: 109 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.22405

Proteins 76:255-260 (2009)

PubMed id: 19338061

Solution structure and glycophorin C binding studies of the protein 4.1R FERM alpha-lobe domain.

H.Kusunoki, T.Kohno.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Solution structure of the 4.1R -lobe domain. (A) Stereo view of the 20 final structures of the 4.1R -lobe domain. The superposition of the backbone atoms (N, C , and C ) is shown. (B) Ribbon diagram of the final lowest energy structure of the 4.1R -lobe domain. The secondary structure elements are labeled. (C) Superposition of the NMR structure determined in this study (green) with the crystal structure of the -lobe domain (blue) in the 4.1R FERM domain (PDB code 1GG3).[9] The N-lobe domain is shown in yellow, the -lobe domain in blue, and the C-lobe domain in red. (D) Identification of the GPC-binding site on the 4.1R -lobe domain. The orientation of the left image in this panel is the same as that in panel B. The right image in this panel is related to that in the left image by a 180° rotation along the vertical axis. The residues showing large chemical shift changes ( z0.1 ppm), caused by the addition of a 10-fold molar excess of GPC, (82-128) are colored red. Almost all of these residues reside on one side of the protein surface. The ELEE motif is colored orange.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 76, 255-260) copyright 2009.