1edm

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(New page: 200px<br /> <applet load="1edm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edm, resolution 1.5&Aring;" /> '''EPIDERMAL GROWTH FAC...)
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'''EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX'''<br />
'''EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX'''<br />
==Overview==
==Overview==
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Various diverse extracellular proteins possess Ca(2+)-binding epidermal, growth factor (EGF)-like domains, the function of which remains uncertain., We have determined, at high resolution (1.5 A), the crystal structure of, such a domain, from human clotting factor IX, as a complex with Ca2+. The, Ca2+ ligands form a classic pentagonal bipyramid with six ligands, contributed by one polypeptide chain and the seventh supplied by a, neighboring EGF-like domain. The crystal structure identifies the role of, Ca2+ in maintaining the conformation of the N-terminal region of the, domain, but more importantly demonstrates that Ca2+ can directly mediate, protein-protein contacts. The observed crystal packing of the domains, provides a plausible model for the association of multiple tandemly linked, EGF-like domains in proteins such as fibrillin-1, Notch, and protein S., This model is consistent with the known functional data and suggests a, general biological role for these domains.
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Various diverse extracellular proteins possess Ca(2+)-binding epidermal growth factor (EGF)-like domains, the function of which remains uncertain. We have determined, at high resolution (1.5 A), the crystal structure of such a domain, from human clotting factor IX, as a complex with Ca2+. The Ca2+ ligands form a classic pentagonal bipyramid with six ligands contributed by one polypeptide chain and the seventh supplied by a neighboring EGF-like domain. The crystal structure identifies the role of Ca2+ in maintaining the conformation of the N-terminal region of the domain, but more importantly demonstrates that Ca2+ can directly mediate protein-protein contacts. The observed crystal packing of the domains provides a plausible model for the association of multiple tandemly linked EGF-like domains in proteins such as fibrillin-1, Notch, and protein S. This model is consistent with the known functional data and suggests a general biological role for these domains.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1EDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EDM OCA].
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1EDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDM OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brownlee, G.G.]]
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[[Category: Brownlee, G G.]]
[[Category: Handford, P.]]
[[Category: Handford, P.]]
[[Category: Knott, V.]]
[[Category: Knott, V.]]
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[[Category: structure and function]]
[[Category: structure and function]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:42:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:36 2008''

Revision as of 10:26, 21 February 2008


1edm, resolution 1.5Å

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EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX

Contents

Overview

Various diverse extracellular proteins possess Ca(2+)-binding epidermal growth factor (EGF)-like domains, the function of which remains uncertain. We have determined, at high resolution (1.5 A), the crystal structure of such a domain, from human clotting factor IX, as a complex with Ca2+. The Ca2+ ligands form a classic pentagonal bipyramid with six ligands contributed by one polypeptide chain and the seventh supplied by a neighboring EGF-like domain. The crystal structure identifies the role of Ca2+ in maintaining the conformation of the N-terminal region of the domain, but more importantly demonstrates that Ca2+ can directly mediate protein-protein contacts. The observed crystal packing of the domains provides a plausible model for the association of multiple tandemly linked EGF-like domains in proteins such as fibrillin-1, Notch, and protein S. This model is consistent with the known functional data and suggests a general biological role for these domains.

Disease

Known diseases associated with this structure: Hemophilia B OMIM:[306900], Warfarin sensitivity OMIM:[306900]

About this Structure

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

Reference

The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions., Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stuart D, Cell. 1995 Jul 14;82(1):131-41. PMID:7606779

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