1qp1
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1bre|1BRE]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qp1 OCA], [http://www.ebi.ac.uk/pdbsum/1qp1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qp1 RCSB]</span> | ||
}} | }} | ||
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[[Category: double spiral]] | [[Category: double spiral]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:59 2008'' |
Revision as of 20:17, 30 March 2008
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| , resolution 2.06Å | |||||||
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| Related: | 1BRE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 1999 Feb;125(2):422-9. PMID:9990143
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