2j5w

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{{STRUCTURE_2j5w| PDB=2j5w | SCENE= }}
{{STRUCTURE_2j5w| PDB=2j5w | SCENE= }}
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'''CERULOPLASMIN REVISITED: STRUCTURAL AND FUNCTIONAL ROLES OF VARIOUS METAL CATION BINDING SITES'''
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===CERULOPLASMIN REVISITED: STRUCTURAL AND FUNCTIONAL ROLES OF VARIOUS METAL CATION BINDING SITES===
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==Overview==
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The three-dimensional molecular structure of human serum ceruloplasmin has been reinvestigated using X-ray synchrotron data collected at 100 K from a crystal frozen to liquid-nitrogen temperature. The resulting model, with an increase in resolution from 3.1 to 2.8 A, gives an overall improvement of the molecular structure, in particular the side chains. In addition, it enables the clear definition of previously unidentified Ca2+-binding and Na+-binding sites. The Ca2+ cation is located in domain 1 in a configuration very similar to that found in the activated bovine factor Va. The Na+ sites appear to play a structural role in providing rigidity to the three protuberances on the top surface of the molecule. These features probably help to steer substrates towards the mononuclear copper sites prior to their oxidation and to restrict the size of the approaching substrate. The trinuclear copper centre appears to differ from the room-temperature structure in that a dioxygen moiety is bound in a similar way to that found in the endospore coat protein CotA from Bacillus subtilis.
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(as it appears on PubMed at http://www.pubmed.gov), where 17242517 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17242517}}
==About this Structure==
==About this Structure==
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[[Category: Polymorphism]]
[[Category: Polymorphism]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:23:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:51:47 2008''

Revision as of 19:51, 28 July 2008

Image:2j5w.png

Template:STRUCTURE 2j5w

CERULOPLASMIN REVISITED: STRUCTURAL AND FUNCTIONAL ROLES OF VARIOUS METAL CATION BINDING SITES

Template:ABSTRACT PUBMED 17242517

About this Structure

2J5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites., Bento I, Peixoto C, Zaitsev VN, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):240-8. Epub 2007, Jan 16. PMID:17242517

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