PDBsum entry 1fna

Cell adhesion protein

PDB id: 1fna

Contents

Protein chain

91 a.a. *

* Residue conservation analysis

PDB id:

1fna

Name:

Cell adhesion protein

Title:

Crystal structure of the tenth type iii cell adhesion module of human fibronectin

Structure:

Fibronectin cell-adhesion module type iii-10. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

Resolution:

1.80Å R-factor: 0.180

Authors:

C.D.Dickinson,B.Veerapandian,K.R.Ely

Key ref:

C.D.Dickinson et al. (1994). Crystal structure of the tenth type III cell adhesion module of human fibronectin. J Mol Biol, 236, 1079-1092. PubMed id: 8120888 DOI: 10.1016/0022-2836(94)90013-2

Date:

11-Jan-94 Release date: 30-Apr-94

Protein chain

P02751  (FINC_HUMAN) -  Fibronectin from Homo sapiens

Seq: 2477 a.a.

Struc: 91 a.a.

DOI no: 10.1016/0022-2836(94)90013-2

J Mol Biol 236:1079-1092 (1994)

PubMed id: 8120888

Crystal structure of the tenth type III cell adhesion module of human fibronectin.

C.D.Dickinson, B.Veerapandian, X.P.Dai, R.C.Hamlin, N.H.Xuong, E.Ruoslahti, K.R.Ely.

ABSTRACT

The crystal structure of the cell adhesion module of fibronectin (FNIII10) has been determined at 1.8 A resolution. A recombinant fragment corresponding to the tenth type III module of human fibronectin was crystallized in space group P2(1) with a = 30.7, b = 35.1 and c = 37.7 A and beta = 107 degrees. The structure was determined by molecular replacement and refined by least squares methods. The crystallographic R-factor for the final model of the 91 amino acid module plus 56 solvent atoms is 0.18 for 10 to 1.8 A data. The module consists of two layers of beta-sheet, one with three antiparallel strands and the other with four antiparallel strands. The beta-sheets enclose a hydrophobic core of 24 amino acid side-chains. The module contains the RGD cell recognition sequence in a flexible loop connecting two beta-strands. The tertiary structure of the FNIII10 module has been used to develop a structure-based sequence alignment of 17 type III modules in fibronectin based on the striking conservation of homologous hydrophobic residues. A similar pattern of homologous alternating hydrophobic residues is also evident in a comparison of type III modules in proteins unrelated to fibronectin such as cytokine receptors and muscle proteins.

Selected figure(s)

Figure 5.
Figure 5. The secondary structures were identified using the procedure of Kabsch & Sander (1983), except that stran B was lengthened by two residues (t, Asp23) and an additional J-turn, hrl4- Serl7, was identified by inspection. Hydrogen bonds between main-chain atoms that stabilize the P-sheets are shown graphically n he stereoplot n Figure 6, and are tabulated in Table 3. Hydrogen bonds involving side-chain atoms are listed n Table 4. A /?-bulge is present in the N-terminal strand that interrupts the regular hydrogen onding pattern n strand A: main-hain hydrogen bonds ccw between residues Valll and Ala12 and Leul9 of strand see ig. 6). The conformational torsion angles or Vail 1 4 = - 90, cp = - 20) are similar to thse observed in the NMR anlysis (Main et al., 1992) ndicating that this ``bulge'' is a stable struc- tural feature of the NIII,o module.

Figure 10.
Figure 10. Comparison of the tertiary folding pattern of type III modules from tibronect.in and tensc*in. The a-carbon backbone of FKIII,, (heavy lines) is superimposed on the a-carbon backbone of tenasrin TNfn3-3 (I,eabT / 1.. I!1!):!) shown with thin lines. Pu'umbers correspond to the F~TII,, sequence. The models were superimposed in his orientation with an r.m.s. difference of I.07 L% for 73 eouivalent a-carbons. indicating the structural similarity f backbone atoms fol these 2 type III modules.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1994, 236, 1079-1092) copyright 1994.

Figures were selected by an automated process.