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1zon

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{{STRUCTURE_1zon| PDB=1zon | SCENE= }}
{{STRUCTURE_1zon| PDB=1zon | SCENE= }}
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'''CD11A I-DOMAIN WITHOUT BOUND CATION'''
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===CD11A I-DOMAIN WITHOUT BOUND CATION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8805579 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8805579}}
==About this Structure==
==About this Structure==
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[[Category: Signal]]
[[Category: Signal]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:17:14 2008''

Revision as of 01:17, 28 July 2008

Image:1zon.png

Template:STRUCTURE 1zon

CD11A I-DOMAIN WITHOUT BOUND CATION

Template:ABSTRACT PUBMED 8805579

About this Structure

1ZON 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 Jul 28 04:17:14 2008

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