1bre
From Proteopedia
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| - | [[Image:1bre.gif|left|200px]] | + | [[Image:1bre.gif|left|200px]] |
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| - | '''IMMUNOGLOBULIN LIGHT CHAIN PROTEIN''' | + | {{Structure |
| + | |PDB= 1bre |SIZE=350|CAPTION= <scene name='initialview01'>1bre</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CDNA (GENBANK ACCESSION CODE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''IMMUNOGLOBULIN LIGHT CHAIN PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BRE is a [ | + | 1BRE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRE OCA]. |
==Reference== | ==Reference== | ||
| - | Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation., Schormann N, Murrell JR, Liepnieks JJ, Benson MD, Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9490-4. PMID:[http:// | + | Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation., Schormann N, Murrell JR, Liepnieks JJ, Benson MD, Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9490-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7568160 7568160] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:14:46 2008'' |
Revision as of 08:14, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Gene: | CDNA (GENBANK ACCESSION CODE (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
IMMUNOGLOBULIN LIGHT CHAIN PROTEIN
Overview
An immunoglobulin light chain protein was isolated from the urine of an individual (BRE) with systemic amyloidosis. Complete amino acid sequence of the variable region of the light chain (VL) protein established it as a kappa I, which when compared with other kappa I amyloid associated proteins had unique residues, including Ile-34, Leu-40, and Tyr-71. To study the tertiary structure, BRE VL was expressed in Escherichia coli by using a PCR product amplified from the patient BRE's bone marrow DNA. The PCR product was ligated into pCZ11, a thermal-inducible replication vector. Recombinant BRE VL was isolated, purified to homogeneity, and crystallized by using ammonium sulfate as the precipitant. Two crystal forms were obtained. In crystal form I the BRE VL kappa domain crystallizes as a dimer with unit cell constants isomorphous to previously published kappa protein structures. Comparison with a nonamyloid VL kappa domain from patient REI, identified significant differences in position of residues in the hypervariable segments plus variations in framework region (FR) segments 40-46 (FR2) and 66-67 (FR3). In addition, positional differences can be seen along the two types of local diads, corresponding to the monomer-monomer and dimer-dimer interfaces. From the packing diagram, a model for the amyloid light chain (AL) fibril is proposed based on a pseudohexagonal spiral structure with a rise of approximately the width of two dimers per 360 degree turn. This spiral structure could be consistent with the dimensions of amyloid fibrils as determined by electron microscopy.
About this Structure
1BRE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation., Schormann N, Murrell JR, Liepnieks JJ, Benson MD, Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9490-4. PMID:7568160
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