1f6l
From Proteopedia
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| - | [[Image:1f6l.gif|left|200px]] | + | [[Image:1f6l.gif|left|200px]] |
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| - | '''VARIABLE LIGHT CHAIN DIMER OF ANTI-FERRITIN ANTIBODY''' | + | {{Structure |
| + | |PDB= 1f6l |SIZE=350|CAPTION= <scene name='initialview01'>1f6l</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''VARIABLE LIGHT CHAIN DIMER OF ANTI-FERRITIN ANTIBODY''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F6L is a [ | + | 1F6L 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=1F6L OCA]. |
==Reference== | ==Reference== | ||
| - | Antiferritin VL homodimer binds human spleen ferritin with high specificity., Nymalm Y, Kravchuk Z, Salminen T, Chumanevich AA, Dubnovitsky AP, Kankare J, Pentikainen O, Lehtonen J, Arosio P, Martsev S, Johnson MS, J Struct Biol. 2002 Jun;138(3):171-86. PMID:[http:// | + | Antiferritin VL homodimer binds human spleen ferritin with high specificity., Nymalm Y, Kravchuk Z, Salminen T, Chumanevich AA, Dubnovitsky AP, Kankare J, Pentikainen O, Lehtonen J, Arosio P, Martsev S, Johnson MS, J Struct Biol. 2002 Jun;138(3):171-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12217656 12217656] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: variable light chain]] | [[Category: variable light chain]] | ||
| - | ''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 11:05:06 2008'' |
Revision as of 09:05, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
VARIABLE LIGHT CHAIN DIMER OF ANTI-FERRITIN ANTIBODY
Overview
The antiferritin variable light domain (VL) dimer binds human spleen ferritin ( approximately 85% L subunits) but with approximately 50-fold lower affinity, K(a)=4 x 10(7) x M(-1), than the parent F11 antibody (K(a)=2.1 x 10(9) x M(-1)). The VL dimer does not recognize either rL (100% L subunits) or rH (100% H subunits) human ferritin, whereas the parent antibody recognizes rL-ferritin. To help explain the differences in ferritin binding affinities and specificities, the crystal structure of the VL domain (2.8A resolution) was determined by molecular replacement and models of the antiferritin VL-VH dimer were made on the basis of antilysozyme antibody D1.3. The domain interface is smaller in the VL dimer but a larger number of interdomain hydrogen bonds may prevent rearrangement on antigen binding. The antigen binding surface of the VL dimer is flatter, lacking a negatively charged pocket found in the VL-VH models, contributed by the CDR3 loop of the VH domain. Loop CDR2 (VL dimer) is located away from the antigen binding site, while the corresponding loop of the VH domain would be located within the antigen binding site. Together these differences lead to 50-fold lower binding affinity in the VL dimer and to more restricted specificity than is seen for the parent antibody.
About this Structure
1F6L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Antiferritin VL homodimer binds human spleen ferritin with high specificity., Nymalm Y, Kravchuk Z, Salminen T, Chumanevich AA, Dubnovitsky AP, Kankare J, Pentikainen O, Lehtonen J, Arosio P, Martsev S, Johnson MS, J Struct Biol. 2002 Jun;138(3):171-86. PMID:12217656
Page seeded by OCA on Thu Mar 20 11:05:06 2008
