3hus
From Proteopedia
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[[Image:3hus.png|left|200px]] | [[Image:3hus.png|left|200px]] | ||
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{{ABSTRACT_PUBMED_19650644}} | {{ABSTRACT_PUBMED_19650644}} | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Afibrinogenemia, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Amyloidosis, hereditary renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Afibrinogenemia, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]], Dysfibrinogenemia, beta type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]], Thrombophilia, dysfibrinogenemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]] | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3hus]] is a 10 chain structure of [[Fibrinogen]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HUS OCA]. | |
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| + | ==See Also== | ||
| + | *[[Fibrinogen]] | ||
==Reference== | ==Reference== | ||
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[[Category: Secreted]] | [[Category: Secreted]] | ||
[[Category: Sulfation]] | [[Category: Sulfation]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 23 08:22:54 2009'' | ||
Revision as of 08:52, 26 December 2010
Contents |
Crystal structure of recombinant gamma N308K fibrinogen fragment D with the peptide ligand Gly-Pro-Arg-Pro-amide
Template:ABSTRACT PUBMED 19650644
About this Structure
3hus is a 10 chain structure of Fibrinogen with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Bowley SR, Okumura N, Lord ST. Impaired protofibril formation in fibrinogen N308K is due to altered D:D and A:a interactions. Biochemistry. 2009 Aug 3. PMID:19650644 doi:10.1021/bi900239b
Categories: Homo sapiens | Bowley, S R. | Lord, S T. | Okumura, N. | Alternative splicing | Amyloid | Amyloidosis | Blood clotting | Blood coagulation | Calcium | Coiled coil | Disease mutation | Disulfide bond | Fibrinogen fragment d | Glycoprotein | Isopeptide bond | Phosphoprotein | Polymorphism | Pyrrolidone carboxylic acid | Secreted | Sulfation
