1xo5

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==Overview==
==Overview==
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CIB1 (CIB) is an EF-hand-containing protein that binds multiple effector, proteins, including the platelet alphaIIbbeta3 integrin and several, serine/threonine kinases and potentially modulates their function. The, crystal structure for Ca(2+)-bound CIB1 has been determined at 2.0 A, resolution and reveals a compact alpha-helical protein containing four, EF-hands, the last two of which bind calcium ions in the standard fashion, seen in many other EF-hand proteins. CIB1 shares high structural, similarity with calcineurin B and the neuronal calcium sensor (NCS) family, of EF-hand-containing proteins. Most importantly, like calcineurin B and, NCS proteins, which possess a large hydrophobic pocket necessary for, ligand binding, CIB1 contains a hydrophobic pocket that has been, implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca(2+)-bound CIB1 is largely monomeric, whether bound to a relevant peptide ligand or ligand-free. Differences in, structure, oligomeric state, and phylogeny define a new family of, CIB1-related proteins that extends from arthropods to humans.
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CIB1 (CIB) is an EF-hand-containing protein that binds multiple effector proteins, including the platelet alphaIIbbeta3 integrin and several serine/threonine kinases and potentially modulates their function. The crystal structure for Ca(2+)-bound CIB1 has been determined at 2.0 A resolution and reveals a compact alpha-helical protein containing four EF-hands, the last two of which bind calcium ions in the standard fashion seen in many other EF-hand proteins. CIB1 shares high structural similarity with calcineurin B and the neuronal calcium sensor (NCS) family of EF-hand-containing proteins. Most importantly, like calcineurin B and NCS proteins, which possess a large hydrophobic pocket necessary for ligand binding, CIB1 contains a hydrophobic pocket that has been implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca(2+)-bound CIB1 is largely monomeric whether bound to a relevant peptide ligand or ligand-free. Differences in structure, oligomeric state, and phylogeny define a new family of CIB1-related proteins that extends from arthropods to humans.
==Disease==
==Disease==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Betts, L.]]
[[Category: Betts, L.]]
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[[Category: Ferrara, J.D.]]
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[[Category: Ferrara, J D.]]
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[[Category: Gentry, H.R.]]
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[[Category: Gentry, H R.]]
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[[Category: Parise, L.V.]]
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[[Category: Parise, L V.]]
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[[Category: Singer, A.U.]]
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[[Category: Singer, A U.]]
[[Category: Sondek, J.]]
[[Category: Sondek, J.]]
[[Category: Yang, C.]]
[[Category: Yang, C.]]
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[[Category: kinase interacting protein]]
[[Category: kinase interacting protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:09:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:56 2008''

Revision as of 13:57, 21 February 2008


1xo5, resolution 1.99Å

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Crystal structure of CIB1, an EF-hand, integrin and kinase-binding protein

Contents

Overview

CIB1 (CIB) is an EF-hand-containing protein that binds multiple effector proteins, including the platelet alphaIIbbeta3 integrin and several serine/threonine kinases and potentially modulates their function. The crystal structure for Ca(2+)-bound CIB1 has been determined at 2.0 A resolution and reveals a compact alpha-helical protein containing four EF-hands, the last two of which bind calcium ions in the standard fashion seen in many other EF-hand proteins. CIB1 shares high structural similarity with calcineurin B and the neuronal calcium sensor (NCS) family of EF-hand-containing proteins. Most importantly, like calcineurin B and NCS proteins, which possess a large hydrophobic pocket necessary for ligand binding, CIB1 contains a hydrophobic pocket that has been implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca(2+)-bound CIB1 is largely monomeric whether bound to a relevant peptide ligand or ligand-free. Differences in structure, oligomeric state, and phylogeny define a new family of CIB1-related proteins that extends from arthropods to humans.

Disease

Known disease associated with this structure: Multiple endocrine neoplasia, type IV OMIM:[600778]

About this Structure

1XO5 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins., Gentry HR, Singer AU, Betts L, Yang C, Ferrara JD, Sondek J, Parise LV, J Biol Chem. 2005 Mar 4;280(9):8407-15. Epub 2004 Dec 1. PMID:15574431

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