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1idn

From Proteopedia

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[[Image:1idn.gif|left|200px]]
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{{STRUCTURE_1idn| PDB=1idn | SCENE= }}
{{STRUCTURE_1idn| PDB=1idn | SCENE= }}
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'''MAC-1 I DOMAIN METAL FREE'''
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===MAC-1 I DOMAIN METAL FREE===
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==Overview==
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BACKGROUND: The integrin family of cell-surface receptors mediate cell adhesion through interactions with the extracellular matrix or other cell-surface receptors. The alpha chain of some integrin heterodimers includes an inserted 'I domain' of about 200 amino acids which binds divalent metal ions and is essential for integrin function. Lee et al. proposed that the I domain of the integrin CD11b adopts a unique 'active' conformation when bound to its counter receptor. In addition, they proposed that the lack of adhesion in the presence of Ca2+ ion reflected the stabilization of an 'inactive' I-domain conformation. We set out to independently determine the structure of the CD11 b I domain and to evaluate the structural effects of divalent ion binding to this protein. RESULTS: We have determined the X-ray structure of a new crystal form of the CD11 b I domain in the absence of added metal ions by multiple isomorphous replacement (MIR). Metal ions were easily introduced into this crystal form allowing the straight-forward assessment of the structural effects of divalent cation binding at the metal ion dependent adhesion site (MIDAS). The equilibrium binding constants for these ions were determined by titration calorimetry. The overall protein conformation and metal-ion coordination of the I domain is the same as that observed for all previously reported CD11 a I-domain structures and a CD11 b I-domain complex with Mn2+. These structures define a majority conformation. CONCLUSIONS: Addition of the cations Mg2+, Mn2+ and Cd2+ to the metal-free I domain does not induce conformational changes in the crystalline environment. Moreover, we find that Ca2+ binds poorly to the I domain which serves to explain its failure to support adhesion. We show that the active conformation proposed by Lee et al, is likely to be a construct artifact and we propose that the currently available data do not support a dramatic structural transition for the I domain during counter-receptor binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 9687375 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9687375}}
==About this Structure==
==About this Structure==
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[[Category: I domain]]
[[Category: I domain]]
[[Category: Integrin]]
[[Category: Integrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:48:30 2008''

Revision as of 07:48, 1 July 2008

Image:1idn.png

Template:STRUCTURE 1idn

MAC-1 I DOMAIN METAL FREE

Template:ABSTRACT PUBMED 9687375

About this Structure

1IDN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Cation binding to the integrin CD11b I domain and activation model assessment., Baldwin ET, Sarver RW, Bryant GL Jr, Curry KA, Fairbanks MB, Finzel BC, Garlick RL, Heinrikson RL, Horton NC, Kelley LL, Mildner AM, Moon JB, Mott JE, Mutchler VT, Tomich CS, Watenpaugh KD, Wiley VH, Structure. 1998 Jul 15;6(7):923-35. PMID:9687375

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