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1QR4

TWO FIBRONECTIN TYPE-III DOMAIN SEGMENT FROM CHICKEN TENASCIN

Summary for 1QR4
Entry DOI10.2210/pdb1qr4/pdb
DescriptorPROTEIN (TENASCIN) (2 entities in total)
Functional Keywordstenascin, fibronectin type-iii, heparin, extracellular matrix, adhesion, fusion protein, structural protein
Biological sourceGallus gallus (chicken)
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Total number of polymer chains2
Total formula weight40521.68
Authors
Piontek, K.,Bisig, D.A. (deposition date: 1999-06-17, release date: 1999-06-28, Last modification date: 2023-08-16)
Primary citationBisig, D.,Weber, P.,Vaughan, L.,Winterhalter, K.H.,Piontek, K.
Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions.
Acta Crystallogr.,Sect.D, 55:1069-1073, 1999
Cited by
PubMed Abstract: A fragment of chicken tenascin consisting of fibronectin type-III domains 5 and 6 has been expressed in Escherichia coli. After modifying a previously reported purification protocol, an electrophoretically homogeneous recombinant protein was obtained from which various crystal forms could be grown under identical conditions. Only one form was suitable for structure determination. These crystals belong to space group P21, with unit-cell parameters a = 45.2, b = 57.9, c = 72.2 A, beta = 91.4 degrees, and diffract to at least 2.6 A resolution using synchrotron radiation. From density measurements of the crystals, it was found that there are two molecules in the asymmetric unit. Diffraction data of native, two platinum-derivative and one palladium-derivative crystals were collected.
PubMed: 10216309
DOI: 10.1107/S090744499900284X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

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