1faw: Difference between revisions

Revision as of 02:58, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1faw.png

Template:STRUCTURE 1faw

GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)

Template:ABSTRACT PUBMED 11717498

About this StructureAbout this Structure

1FAW is a Protein complex structure of sequences from Anser anser. Full crystallographic information is available from OCA.

ReferenceReference

The structure of greylag goose oxy haemoglobin: the roles of four mutations compared with bar-headed goose haemoglobin., Liang YH, Liu XZ, Liu SH, Lu GY, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1850-6. Epub 2001, Nov 21. PMID:11717498

Page seeded by OCA on Tue Jul 1 02:58:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1faw.jpg|left|200px]]
+{{Seed}}
+[[Image:1faw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1faw|  PDB=1faw  |  SCENE=  }}
-'''GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)'''
+===GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)===
-==Overview==
+<!--
-The greylag goose (Anser anser), which lives on lowlands and cannot tolerate hypoxic conditions, presents a striking contrast to its close relative the bar-headed goose (A. indicus), which lives at high altitude and possesses high-altitude hypoxia adaptation. There are only four amino-acid residue differences at alpha18, alpha63, alpha119 and beta125 between the haemoglobins of the two species. The crystal structure of greylag goose oxy haemoglobin was determined at 3.09 A resolution. Its quaternary structure is slightly different from that of the bar-headed goose oxy haemoglobin, with a rotation of 2.8 degrees in relative orientation of the two dimers. Of the four mutations, those at alpha119 and beta125 produce contact changes in the alpha(1)beta(1) interface and may be responsible for the differences in intrinsic oxygen affinity between the two species; those at alpha18 and alpha63 may be responsible for the differences in quaternary structure between the two species.
+The line below this paragraph, {{ABSTRACT_PUBMED_11717498}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11717498 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11717498}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Oxygen transport]]
 [[Category: Respiratory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:06:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:58:27 2008''