2oyh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 23: | Line 23: | ||
==About this Structure== | ==About this Structure== | ||
2OYH is a | 2OYH is a 10 chains structure of sequences 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=2OYH OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:17411074</ref><references group="xtra"/> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Gorkun, O V.]] | [[Category: Gorkun, O V.]] | ||
[[Category: Kostelansky, M S.]] | [[Category: Kostelansky, M S.]] | ||
| Line 38: | Line 37: | ||
[[Category: Variant fibrinogen]] | [[Category: Variant fibrinogen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:57:08 2009'' | ||
Revision as of 18:57, 17 February 2009
Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-AmideCrystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide
Template:ABSTRACT PUBMED 17411074
DiseaseDisease
Known disease associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820], Afibrinogenemia, congenital OMIM:[134830], Dysfibrinogenemia, beta type OMIM:[134830], Thrombophilia, dysfibrinogenemic OMIM:[134830], Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134850]
About this StructureAbout this Structure
2OYH is a 10 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Kostelansky MS, Lounes KC, Ping LF, Dickerson SK, Gorkun OV, Lord ST. Probing the gamma2 calcium-binding site: studies with gammaD298,301A fibrinogen reveal changes in the gamma294-301 loop that alter the integrity of the "a" polymerization site. Biochemistry. 2007 May 1;46(17):5114-23. Epub 2007 Apr 6. PMID:17411074 doi:10.1021/bi602607a
Page seeded by OCA on Tue Feb 17 17:57:08 2009