1qp1

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(New page: 200px<br /> <applet load="1qp1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qp1, resolution 2.06&Aring;" /> '''KAPPA VARIABLE LIGH...)
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Revision as of 07:33, 18 November 2007


1qp1, resolution 2.06Å

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KAPPA VARIABLE LIGHT CHAIN

Overview

The molecular structure of the amyloid-forming Bence-Jones protein kappa I, Bre has been determined by X-ray crystallography at 2.0 A resolution. The, fragment from the kappa chain of immunoprotein contains 107 amino acid, residues, and polymerizes in the crystal form into a giant helical spiral, surrounding a cylinder of water 50 A in diameter with a repeat of 77.56 A, containing 12 kappa molecules, plus another 12 molecules from neighboring, parallel spirals. The resulting structure has many features which have, been found or suggested from studies on the protein fibrils found in, amyloid deposits. From the results of the X-ray crystal structure a, hypothesis is presented for the structure and formation of the amyloid, fibril.

About this Structure

1QP1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular structure of the amyloid-forming protein kappa I Bre., Steinrauf LK, Chiang MY, Shiuan D, J Biochem (Tokyo). 1999 Feb;125(2):422-9. PMID:9990143

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