PDBsum entry 3ehr

Signaling protein

PDB id: 3ehr

Contents

Protein chain

178 a.a. *

Waters ×359

* Residue conservation analysis

PDB id:

3ehr

Name:

Signaling protein

Title:

Crystal structure of human osteoclast stimulating factor

Structure:

Osteoclast-stimulating factor 1. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ostf1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.95Å R-factor: 0.181 R-free: 0.239

Authors:

S.Tong,H.Zhou,Y.Gao,Z.Zhu,X.Zhang,M.Teng,L.Niu

Key ref:

S.Tong et al. (2009). Crystal structure of human osteoclast stimulating factor. Proteins, 75, 245-251. PubMed id: 19137598 DOI: 10.1002/prot.22333

Date:

14-Sep-08 Release date: 04-Aug-09

Protein chains

Q92882  (OSTF1_HUMAN) -  Osteoclast-stimulating factor 1 from Homo sapiens

Seq: 214 a.a.

Struc: 178 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1002/prot.22333

Proteins 75:245-251 (2009)

PubMed id: 19137598

Crystal structure of human osteoclast stimulating factor.

S.Tong, H.Zhou, Y.Gao, Z.Zhu, X.Zhang, M.Teng, L.Niu.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. (A) Ribbon representation of human OSF (chain B, crystal form II). Standard numbering of the secondary elements is indicated. (B) Ribbon representation of human OSF in two crystal forms with SH3 domain aligned only. (Magenta for crystal form I, green for crystal form II.) (C) Sequence alignment of OSF SH3 domain with some other SH3 domains. Secondary structural elements of human OSF-SH3 were shown above the alignment and Abl SH3 domain secondary structural elements were shown below. Conserved residues involving peptide binding are marked by * . (D) Structure-based sequence alignment of OSF ankyrin repeats domain with some other ankyrin repeats. Secondary structural elements of human OSF ankyrin repeats were shown above the alignment. Numbers above the sequences correspond to the OSF sequence.

Figure 2.
Figure 2. Stereodiagram view of the superposition of 1SEM (green), 1ZLM (magenta) and our OSF-SH3 (slate blue) with (A) the conserved residues of OSF-SH3 for peptide binding were labeled and shown in stick, and (B) the binding pocket of peptide residue arginine. Arg26 and Glu30 of OSF-SH3 domain were labeled and shown in stick view. Ligand peptide Ace-PPPVPPR (red) of 1SEM was shown in line view in (A) and in stick view in (B). (C) The putative binding interface of OSF ankyrin repeats. Left: Electrostatic potential distribution on the potential binding surface of OSF ankyrin repeats. Right: Stick view of residues comprising the putative binding surface at the same orientation.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 75, 245-251) copyright 2009.