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1zop
From Proteopedia
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|PDB= 1zop |SIZE=350|CAPTION= <scene name='initialview01'>1zop</scene>, resolution 2.0Å | |PDB= 1zop |SIZE=350|CAPTION= <scene name='initialview01'>1zop</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PCR PRODUCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PCR PRODUCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zop OCA], [http://www.ebi.ac.uk/pdbsum/1zop PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zop RCSB]</span> | ||
}} | }} | ||
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[[Category: Leahy, D J.]] | [[Category: Leahy, D J.]] | ||
[[Category: Qu, A.]] | [[Category: Qu, A.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MN]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:39:38 2008'' |
Revision as of 22:39, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PCR PRODUCT (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
Overview
BACKGROUND: The integrin family of cell-surface receptors mediates a wide variety of cell-cell and cell-extracellular matrix interactions. Integrin-ligand interactions are invariably dependent on the presence of divalent cations, and a subset of integrins contain a approximately 200 amino acid inserted (I) domain that is important for ligand binding activity and contains a single divalent cation binding site. Many integrins are believed to respond to stimuli by undergoing a conformational change that increases their affinity for ligand, and there is a clear difference between two crystal structures of the CD11b I domain with different divalent cations (magnesium and manganese) bound. In addition to the different bound cation, a 'ligand mimetic' crystal lattice interaction in the CD11b I domain structure with bound magnesium has led to the interpretation that the different CD11b I domain structures represent different affinity states of I domains. The influence of the bound cation on I domain structure and function remains incompletely understood, however. The crystal structure of the CD11a I domain bound to manganese is known. We therefore set out to determine whether this structure changes when the metal ion is altered or removed. RESULTS: We report here the crystal structures of the CD11a I domain determined in the absence of bound metal ion and with bound magnesium ion. No major structural rearrangements are observed in the metal-binding site of the CD11a I domain in the absence or presence of bound manganese ion. The structures of the CD11a I domain with magnesium or manganese bound are extremely similar. CONCLUSIONS: The conformation of the CD11a I domain is not altered by changes in metal ion binding. The cation-dependence of ligand binding thus indicates that the metal ion is either involved in direct interaction with ligand or required to promote a favorable quaternary arrangement of the integrin.
About this Structure
1ZOP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin., Qu A, Leahy DJ, Structure. 1996 Aug 15;4(8):931-42. PMID:8805579
Page seeded by OCA on Mon Mar 31 01:39:38 2008
