1lom
From Proteopedia
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|PDB= 1lom |SIZE=350|CAPTION= <scene name='initialview01'>1lom</scene>, resolution 1.72Å | |PDB= 1lom |SIZE=350|CAPTION= <scene name='initialview01'>1lom</scene>, resolution 1.72Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3ezm|3EZM]], [[1l5b|1L5B]], [[1l5e|1L5E]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lom OCA], [http://www.ebi.ac.uk/pdbsum/1lom PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lom RCSB]</span> | ||
}} | }} | ||
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[[Category: Mori, T.]] | [[Category: Mori, T.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: SO4]] | ||
[[Category: cyanovirin-n]] | [[Category: cyanovirin-n]] | ||
[[Category: domain-swapping]] | [[Category: domain-swapping]] | ||
| Line 34: | Line 35: | ||
[[Category: hiv-inactivating]] | [[Category: hiv-inactivating]] | ||
| - | ''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 22:05:22 2008'' |
Revision as of 19:05, 30 March 2008
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| , resolution 1.72Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 3EZM, 1L5B, 1L5E
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYANOVIRIN-N DOUBLE MUTANT P51S S52P
Overview
Cyanovirin-N (CV-N) is a potent 11 kDa HIV-inactivating protein that binds with high affinity to the HIV surface envelope protein gp120. A double mutant P51S/S52P of CV-N was engineered by swapping two critical hinge-region residues Pro51 and Ser52. This mutant has biochemical and biophysical characteristics equivalent to the wild-type CV-N and its structure resembles that of wild-type CV-N. However, the mutant shows a different orientation in the hinge region that connects two domains of the protein. The observation that this double mutant crystallizes under a wide variety of conditions challenges some of the current hypotheses on domain swapping and on the role of hinge-region proline residues in domain orientation. The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain-swapped CV-N mutants.
About this Structure
1LOM is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Domain-swapped structure of a mutant of cyanovirin-N., Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A, Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761
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